TY  - CONF
AU  - Jovanović, Zorana
AU  - Gligorijević, Nikola
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Nikolić, Milan
AU  - Pavlović, Vladimir
AU  - Lević, Steva
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7607
AB  - C-Phycocyanin (C-PC), the natural blue dye and the major protein in Spirulina, has high potential in the food industry due to its vivid colour and bioactive properties. However, low stability limits C-PC application potential, requiring approaches to strengthen its stability. Our study aimed to preserve C-PC by its incorporation into hydrogels formed by combining starch and β-lactoglobulin (BLG) using high-pressure (HP) processing. Notably, thermal treatment resulted in the complete loss of colour derived from C-PC. We performed a comprehensive characterization of the resulting HP gels by rheology measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and scanning electron microscopy (SEM). Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC) systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7, maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations of components were retained in the binary systems. Rheological properties of the gels were determined using a rheometer with plane/plane geometry, and texture analysis was conducted through TPA. These findings enabled the assessment of food gel’s properties, such as hardness, springiness, chewiness, and cohesiveness. The structural characteristics of the gels were determined by SAXS, offering insights into the interactions between C-PC, BLG, and starch after HP processing. Adding C-PC and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the gel surface revealed that all components influenced the overall morphology of gels. Adding starch notably influenced the gels’ visual appearance and mechanical properties, even at low concentrations. Interestingly, the presence of C-PC substantially increases the gel’s solubility in water. Our investigation highlights HP treatment’s superior effectiveness in preserving C-PC compared to high temperature treatment, evidenced by the sustained colour integrity of the C-PC blue chromophore.
PB  - International Hellenic University
C3  - Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki
T1  - The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin
SP  - 267
EP  - 267
UR  - https://hdl.handle.net/21.15107/rcub_cer_7607
ER  - 

@conference{
author = "Jovanović, Zorana and Gligorijević, Nikola and Annighöfer, Burkhard and Dudzinski, Daniel and Nikolić, Milan and Pavlović, Vladimir and Lević, Steva and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2024",
abstract = "C-Phycocyanin (C-PC), the natural blue dye and the major protein in Spirulina, has high potential in the food industry due to its vivid colour and bioactive properties. However, low stability limits C-PC application potential, requiring approaches to strengthen its stability. Our study aimed to preserve C-PC by its incorporation into hydrogels formed by combining starch and β-lactoglobulin (BLG) using high-pressure (HP) processing. Notably, thermal treatment resulted in the complete loss of colour derived from C-PC. We performed a comprehensive characterization of the resulting HP gels by rheology measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and scanning electron microscopy (SEM). Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC) systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7, maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations of components were retained in the binary systems. Rheological properties of the gels were determined using a rheometer with plane/plane geometry, and texture analysis was conducted through TPA. These findings enabled the assessment of food gel’s properties, such as hardness, springiness, chewiness, and cohesiveness. The structural characteristics of the gels were determined by SAXS, offering insights into the interactions between C-PC, BLG, and starch after HP processing. Adding C-PC and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the gel surface revealed that all components influenced the overall morphology of gels. Adding starch notably influenced the gels’ visual appearance and mechanical properties, even at low concentrations. Interestingly, the presence of C-PC substantially increases the gel’s solubility in water. Our investigation highlights HP treatment’s superior effectiveness in preserving C-PC compared to high temperature treatment, evidenced by the sustained colour integrity of the C-PC blue chromophore.",
publisher = "International Hellenic University",
journal = "Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki",
title = "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin",
pages = "267-267",
url = "https://hdl.handle.net/21.15107/rcub_cer_7607"
}

Jovanović, Z., Gligorijević, N., Annighöfer, B., Dudzinski, D., Nikolić, M., Pavlović, V., Lević, S., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2024). The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki
International Hellenic University., 267-267.
https://hdl.handle.net/21.15107/rcub_cer_7607

Jovanović Z, Gligorijević N, Annighöfer B, Dudzinski D, Nikolić M, Pavlović V, Lević S, Brûlet A, Assifaoui A, Combet S, Minić S. The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki. 2024;:267-267.
https://hdl.handle.net/21.15107/rcub_cer_7607 .

Jovanović, Zorana, Gligorijević, Nikola, Annighöfer, Burkhard, Dudzinski, Daniel, Nikolić, Milan, Pavlović, Vladimir, Lević, Steva, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin" in Food Colloids Conference, Using colloid science to find new sustainable solutions in food, Book of Abstracts, 14-18 April 2024, Thessaloniki (2024):267-267,
https://hdl.handle.net/21.15107/rcub_cer_7607 .

TY  - JOUR
AU  - Radović, Jelena
AU  - Popović, Dragana
AU  - Ćurčić, Tatjana
AU  - Veličković, Luka
AU  - Lević, Steva
AU  - Pavlović, Vladimir
AU  - Minić, Simeon
AU  - Nikolić, Milan
AU  - Gligorijević, Nikola
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7596
AB  - Mercury emissions represent a significant risk to the environment and human health. Mercury is persistent and
can circulate in the environment for thousands of years, which is why treating this toxic metal is important.
Chitosan polymer is easily obtainable, and it has good mercury adsorption characteristics. This study aimed to
improve its capabilities to absorb mercury by immobilizing phycobiliproteins (PBPs) onto the surface of chitosan
beads (chitosan–PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have several
industrially essential applications. These proteins can bind heavy metals with high affinities. Protein extracts
obtained from both Arthrospira platensis, with C-phycocyanin (C-PC) as the primary protein, and Porphyra
yezoensis, with R-phycocyanin (R-PC) and R-phycoerythrin (R-PE) as the dominant PBPs, were covalently
immobilized onto chitosan beads. Beads with immobilized PBPs were characterized by scanning electron microscopy
and Fourier transform infrared spectroscopy. Binding analysis showed that, on average, each chitosan
bead weighed 20 mg and immobilized 63.54 μg of PBPs from Spirulina and 44.12 μg of PBPs from Porphyra.
Immobilized proteins were still in their native state, with no visible color change months after immobilization.
Chitosan–PBPs and chitosan alone were tested for mercury adsorption at pH 4 and pH 7 by atomic absorption
spectroscopy. The tested concentration range of mercury was from 1 to 70 ppm. Affinity, calculated using
Henry’s binding isotherm, of chitosan–PBPs for mercury was twice as much higher at both pH values than
chitosan alone. Furthermore, chitosan-PBP beads were able to absorb more mercury than chitosan alone. These
results showed that the covalent immobilization of PBPs onto chitosan improves its mercury adsorption characteristics
and creates a more efficient eco-friendly adsorbent to potentially remove mercury ions in the tested
concentration range from polluted waters.
PB  - Elsevier
T2  - Algal Research
T1  - Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads
VL  - 80
SP  - 103543
DO  - 10.1016/j.algal.2024.103543
ER  - 

@article{
author = "Radović, Jelena and Popović, Dragana and Ćurčić, Tatjana and Veličković, Luka and Lević, Steva and Pavlović, Vladimir and Minić, Simeon and Nikolić, Milan and Gligorijević, Nikola",
year = "2024",
abstract = "Mercury emissions represent a significant risk to the environment and human health. Mercury is persistent and
can circulate in the environment for thousands of years, which is why treating this toxic metal is important.
Chitosan polymer is easily obtainable, and it has good mercury adsorption characteristics. This study aimed to
improve its capabilities to absorb mercury by immobilizing phycobiliproteins (PBPs) onto the surface of chitosan
beads (chitosan–PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have several
industrially essential applications. These proteins can bind heavy metals with high affinities. Protein extracts
obtained from both Arthrospira platensis, with C-phycocyanin (C-PC) as the primary protein, and Porphyra
yezoensis, with R-phycocyanin (R-PC) and R-phycoerythrin (R-PE) as the dominant PBPs, were covalently
immobilized onto chitosan beads. Beads with immobilized PBPs were characterized by scanning electron microscopy
and Fourier transform infrared spectroscopy. Binding analysis showed that, on average, each chitosan
bead weighed 20 mg and immobilized 63.54 μg of PBPs from Spirulina and 44.12 μg of PBPs from Porphyra.
Immobilized proteins were still in their native state, with no visible color change months after immobilization.
Chitosan–PBPs and chitosan alone were tested for mercury adsorption at pH 4 and pH 7 by atomic absorption
spectroscopy. The tested concentration range of mercury was from 1 to 70 ppm. Affinity, calculated using
Henry’s binding isotherm, of chitosan–PBPs for mercury was twice as much higher at both pH values than
chitosan alone. Furthermore, chitosan-PBP beads were able to absorb more mercury than chitosan alone. These
results showed that the covalent immobilization of PBPs onto chitosan improves its mercury adsorption characteristics
and creates a more efficient eco-friendly adsorbent to potentially remove mercury ions in the tested
concentration range from polluted waters.",
publisher = "Elsevier",
journal = "Algal Research",
title = "Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads",
volume = "80",
pages = "103543",
doi = "10.1016/j.algal.2024.103543"
}

Radović, J., Popović, D., Ćurčić, T., Veličković, L., Lević, S., Pavlović, V., Minić, S., Nikolić, M.,& Gligorijević, N.. (2024). Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads. in Algal Research
Elsevier., 80, 103543.
https://doi.org/10.1016/j.algal.2024.103543

Radović J, Popović D, Ćurčić T, Veličković L, Lević S, Pavlović V, Minić S, Nikolić M, Gligorijević N. Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads. in Algal Research. 2024;80:103543.
doi:10.1016/j.algal.2024.103543 .

Radović, Jelena, Popović, Dragana, Ćurčić, Tatjana, Veličković, Luka, Lević, Steva, Pavlović, Vladimir, Minić, Simeon, Nikolić, Milan, Gligorijević, Nikola, "Probing the potential of mercury removal by covalently immobilized phycobiliproteins onto the surface of chitosan beads" in Algal Research, 80 (2024):103543,
https://doi.org/10.1016/j.algal.2024.103543 . .

TY  - JOUR
AU  - Jovanović, Vesna B.
AU  - Nikolić, Milan
AU  - Stojanović, Srđan
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7828
AB  - In this in silico study, it was investigated whether phycobilins
(phycocyanobilin, phycoerythrobilin and phycourobilin) could be inhibitors of
the activity of the main proteins of the SARS-CoV-2 virus. All chromophores
exhibited a binding energy value of ≥–37 kJ mol-1 for PLpro-WT, PLpro-
-C111S, helicase-ANP binding site, Nsp3-macrodomain, Nsp3-MES site and
Nsp10/14-N7-Mtase. Phycocyanobilin showed the highest binding energy of
–44.77 kJ mol-1 against the target protein PLpro-C111S. It was found that,
apart from the hydrogen bonds and hydrophobic interactions, phycobilins also
form electrostatic interactions with the SARS-CoV-2 proteins. The network of
non-covalent interactions was found to be important for the stability of the
examined virus proteins. All phycobilins have good pharmacokinetic and drug-
-likeness properties. This study’s results suggest that the screened phycobilins
could serve as promising drugs for the treatment of COVID-19 with further
rigorous validation studies.
AB  - У овој in silico студији испитано је да ли би фикобилини (фикоцијанобилин,
фикоеритробилин и фикоуробилин) могли бити инхибитори активности главних
протеина SARS-CoV-2 вируса. Свe хромофоре су показале вредност енергије
везивања ≥ −37 kJ mol-1 према PLpro-WT, PLpro-C111S, хеликаза-ANP везујућем
месту, Nsp3-макродомену, Nsp3-MES месту и Nsp10/14-N7-Mt-ази. Фикоција-
нобилин је показао највећу енергију везивања, од −44,77 kJ mol-1, за циљни про-
теин PLpro-C111S. Утврђено је да, осим водоничних веза и хидрофобних интер-
акција, фикобилини формирају и електростатичке интеракције са SARS-CoV-2 про-
теинима. Пронађена је мрежа нековалентних интеракција важна за стабилност
испитаних вирусних протеина. Сви фикобилини су показали обећавајућа фар-
макокинетичка својства и карактеристике сличне лековима. Резултати овe студије
сугеришу да би, уз додатна ригорозна валидациона испитивања, анализирани
фикобилини могли да послуже као обећавајући лекови за COVID-19.
PB  - Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - In silico studies of phycobilins as potential candidates for inhibitors of viral proteins associated with COVID-19
T1  - In silico студије фикобилина као могућих кандидата за инхибиторе вирусних протеина повезаних са COVID-19
VL  - 89
IS  - 7-8
SP  - 997
EP  - 1009
DO  - 10.2298/JSC240326052J
ER  - 

@article{
author = "Jovanović, Vesna B. and Nikolić, Milan and Stojanović, Srđan",
year = "2024",
abstract = "In this in silico study, it was investigated whether phycobilins
(phycocyanobilin, phycoerythrobilin and phycourobilin) could be inhibitors of
the activity of the main proteins of the SARS-CoV-2 virus. All chromophores
exhibited a binding energy value of ≥–37 kJ mol-1 for PLpro-WT, PLpro-
-C111S, helicase-ANP binding site, Nsp3-macrodomain, Nsp3-MES site and
Nsp10/14-N7-Mtase. Phycocyanobilin showed the highest binding energy of
–44.77 kJ mol-1 against the target protein PLpro-C111S. It was found that,
apart from the hydrogen bonds and hydrophobic interactions, phycobilins also
form electrostatic interactions with the SARS-CoV-2 proteins. The network of
non-covalent interactions was found to be important for the stability of the
examined virus proteins. All phycobilins have good pharmacokinetic and drug-
-likeness properties. This study’s results suggest that the screened phycobilins
could serve as promising drugs for the treatment of COVID-19 with further
rigorous validation studies., У овој in silico студији испитано је да ли би фикобилини (фикоцијанобилин,
фикоеритробилин и фикоуробилин) могли бити инхибитори активности главних
протеина SARS-CoV-2 вируса. Свe хромофоре су показале вредност енергије
везивања ≥ −37 kJ mol-1 према PLpro-WT, PLpro-C111S, хеликаза-ANP везујућем
месту, Nsp3-макродомену, Nsp3-MES месту и Nsp10/14-N7-Mt-ази. Фикоција-
нобилин је показао највећу енергију везивања, од −44,77 kJ mol-1, за циљни про-
теин PLpro-C111S. Утврђено је да, осим водоничних веза и хидрофобних интер-
акција, фикобилини формирају и електростатичке интеракције са SARS-CoV-2 про-
теинима. Пронађена је мрежа нековалентних интеракција важна за стабилност
испитаних вирусних протеина. Сви фикобилини су показали обећавајућа фар-
макокинетичка својства и карактеристике сличне лековима. Резултати овe студије
сугеришу да би, уз додатна ригорозна валидациона испитивања, анализирани
фикобилини могли да послуже као обећавајући лекови за COVID-19.",
publisher = "Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "In silico studies of phycobilins as potential candidates for inhibitors of viral proteins associated with COVID-19, In silico студије фикобилина као могућих кандидата за инхибиторе вирусних протеина повезаних са COVID-19",
volume = "89",
number = "7-8",
pages = "997-1009",
doi = "10.2298/JSC240326052J"
}

Jovanović, V. B., Nikolić, M.,& Stojanović, S.. (2024). In silico studies of phycobilins as potential candidates for inhibitors of viral proteins associated with COVID-19. in Journal of the Serbian Chemical Society
Serbian Chemical Society., 89(7-8), 997-1009.
https://doi.org/10.2298/JSC240326052J

Jovanović VB, Nikolić M, Stojanović S. In silico studies of phycobilins as potential candidates for inhibitors of viral proteins associated with COVID-19. in Journal of the Serbian Chemical Society. 2024;89(7-8):997-1009.
doi:10.2298/JSC240326052J .

Jovanović, Vesna B., Nikolić, Milan, Stojanović, Srđan, "In silico studies of phycobilins as potential candidates for inhibitors of viral proteins associated with COVID-19" in Journal of the Serbian Chemical Society, 89, no. 7-8 (2024):997-1009,
https://doi.org/10.2298/JSC240326052J . .

TY  - JOUR
AU  - Minić, Simeon
AU  - Gligorijević, Nikola
AU  - Veličković, Luka
AU  - Nikolić, Milan
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7687
AB  - Vivid-colored phycobiliproteins (PBPs) have emerging potential as food colors and alternative
proteins in the food industry. However, enhancing their application potential requires increasing
stability, cost-effective purification processes, and consumer acceptance. This narrative review aimed
to highlight information regarding the critical aspects of PBP research that is needed to improve their
food industry potential, such as stability, food fortification, development of new PBP-based food
products, and cost-effective production. The main results of the literature review show that polysaccharide
and protein-based encapsulations significantly improve PBPs’ stability. Additionally, while
many studies have investigated the ability of PBPs to enhance the techno-functional properties, like
viscosity, emulsifying and stabilizing activity, texture, rheology, etc., of widely used food products,
highly concentrated PBP food products are still rare. Therefore, much effort should be invested in
improving the stability, yield, and sensory characteristics of the PBP-fortified food due to the resulting
unpleasant sensory characteristics. Considering that most studies focus on the C-phycocyanin from
Spirulina, future studies should concentrate on less explored PBPs from red macroalgae due to their
much higher production potential, a critical factor for positioning PBPs as alternative proteins.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins
VL  - 25
IS  - 13
SP  - 7187
DO  - 10.3390/ijms25137187
ER  - 

@article{
author = "Minić, Simeon and Gligorijević, Nikola and Veličković, Luka and Nikolić, Milan",
year = "2024",
abstract = "Vivid-colored phycobiliproteins (PBPs) have emerging potential as food colors and alternative
proteins in the food industry. However, enhancing their application potential requires increasing
stability, cost-effective purification processes, and consumer acceptance. This narrative review aimed
to highlight information regarding the critical aspects of PBP research that is needed to improve their
food industry potential, such as stability, food fortification, development of new PBP-based food
products, and cost-effective production. The main results of the literature review show that polysaccharide
and protein-based encapsulations significantly improve PBPs’ stability. Additionally, while
many studies have investigated the ability of PBPs to enhance the techno-functional properties, like
viscosity, emulsifying and stabilizing activity, texture, rheology, etc., of widely used food products,
highly concentrated PBP food products are still rare. Therefore, much effort should be invested in
improving the stability, yield, and sensory characteristics of the PBP-fortified food due to the resulting
unpleasant sensory characteristics. Considering that most studies focus on the C-phycocyanin from
Spirulina, future studies should concentrate on less explored PBPs from red macroalgae due to their
much higher production potential, a critical factor for positioning PBPs as alternative proteins.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins",
volume = "25",
number = "13",
pages = "7187",
doi = "10.3390/ijms25137187"
}

Minić, S., Gligorijević, N., Veličković, L.,& Nikolić, M.. (2024). Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins. in International Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 25(13), 7187.
https://doi.org/10.3390/ijms25137187

Minić S, Gligorijević N, Veličković L, Nikolić M. Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins. in International Journal of Molecular Sciences. 2024;25(13):7187.
doi:10.3390/ijms25137187 .

Minić, Simeon, Gligorijević, Nikola, Veličković, Luka, Nikolić, Milan, "Narrative Review of the Current and Future Perspectives of Phycobiliproteins’ Applications in the Food Industry: From Natural Colors to Alternative Proteins" in International Journal of Molecular Sciences, 25, no. 13 (2024):7187,
https://doi.org/10.3390/ijms25137187 . .

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Jovanović, Zorana
AU  - Cvijetić, Ilija
AU  - Šunderić, Miloš
AU  - Veličković, Luka
AU  - Katrlík, Jaroslav
AU  - Holazová, Alena
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7298
AB  - Blue C-phycocyanin (C-PC), the major Spirulina protein with innumerable
health-promoting benefits, is an attractive colourant and food supplement. A crucial obstacle to its
more extensive use is its relatively low stability. This study aimed to screen various food-derived
ligands for their ability to bind and stabilise C-PC, utilising spectroscopic techniques and molecular
docking. Among twelve examined ligands, the protein fluorescence quenching revealed that
only quercetin, coenzyme Q10 and resveratrol had a moderate affinity to C-PC (Ka of 2.2 to 3.7 × 105
M–1). Docking revealed these three ligands bind more strongly to the C-PC hexamer than the trimer,
with the binding sites located at the interface of two (αβ)3 trimers. UV/VIS absorption spectroscopy
demonstrated the changes in the C-PC absorption spectra in a complex with quercetin
and resveratrol compared to the spectra of free protein and ligands. Selected ligands did not affect
the secondary structure content, but they induced changes in the tertiary protein structure in the
CD study. A fluorescence-based thermal stability assay demonstrated quercetin and coenzyme Q10
increased the C-PC melting point by nearly 5 °C. Our study identified food-derived ligands that
interact with C-PC and improve its thermal stability, indicating their potential as stabilising agents
for C-PC in the food industry.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina
VL  - 25
IS  - 1
SP  - 229
DO  - 10.3390/ijms25010229
ER  - 

@article{
author = "Gligorijević, Nikola and Jovanović, Zorana and Cvijetić, Ilija and Šunderić, Miloš and Veličković, Luka and Katrlík, Jaroslav and Holazová, Alena and Nikolić, Milan and Minić, Simeon",
year = "2024",
abstract = "Blue C-phycocyanin (C-PC), the major Spirulina protein with innumerable
health-promoting benefits, is an attractive colourant and food supplement. A crucial obstacle to its
more extensive use is its relatively low stability. This study aimed to screen various food-derived
ligands for their ability to bind and stabilise C-PC, utilising spectroscopic techniques and molecular
docking. Among twelve examined ligands, the protein fluorescence quenching revealed that
only quercetin, coenzyme Q10 and resveratrol had a moderate affinity to C-PC (Ka of 2.2 to 3.7 × 105
M–1). Docking revealed these three ligands bind more strongly to the C-PC hexamer than the trimer,
with the binding sites located at the interface of two (αβ)3 trimers. UV/VIS absorption spectroscopy
demonstrated the changes in the C-PC absorption spectra in a complex with quercetin
and resveratrol compared to the spectra of free protein and ligands. Selected ligands did not affect
the secondary structure content, but they induced changes in the tertiary protein structure in the
CD study. A fluorescence-based thermal stability assay demonstrated quercetin and coenzyme Q10
increased the C-PC melting point by nearly 5 °C. Our study identified food-derived ligands that
interact with C-PC and improve its thermal stability, indicating their potential as stabilising agents
for C-PC in the food industry.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina",
volume = "25",
number = "1",
pages = "229",
doi = "10.3390/ijms25010229"
}

Gligorijević, N., Jovanović, Z., Cvijetić, I., Šunderić, M., Veličković, L., Katrlík, J., Holazová, A., Nikolić, M.,& Minić, S.. (2024). Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina. in International Journal of Molecular Sciences
MDPI., 25(1), 229.
https://doi.org/10.3390/ijms25010229

Gligorijević N, Jovanović Z, Cvijetić I, Šunderić M, Veličković L, Katrlík J, Holazová A, Nikolić M, Minić S. Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina. in International Journal of Molecular Sciences. 2024;25(1):229.
doi:10.3390/ijms25010229 .

Gligorijević, Nikola, Jovanović, Zorana, Cvijetić, Ilija, Šunderić, Miloš, Veličković, Luka, Katrlík, Jaroslav, Holazová, Alena, Nikolić, Milan, Minić, Simeon, "Investigation of the Potential of Selected Food-Derived Antioxidants to Bind and Stabilise the Bioactive Blue Protein C-Phycocyanin from Cyanobacteria Spirulina" in International Journal of Molecular Sciences, 25, no. 1 (2024):229,
https://doi.org/10.3390/ijms25010229 . .

TY  - JOUR
AU  - Radomirović, Mirjana
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7645
AB  - BACKGROUND: Phycocyanobilin (PCB) is an open-chain blue tetrapyrrole chromophore of C-phycocyanin (C-PC), a major chromoprotein
derived from the cyanobacterium Arthrospira platensis having numerous health-promoting effects. Relying on the
ability of PCB to attach to the sulfhydryl group of proteins, we propose a new method for covalent attachment of PCB to bovine
serum albumin (BSA) as a means of its functionalization.
RESULTS: Traut's reagent (TR, 2-iminothiolane), modifying lysine residues, was used to optimize the introduction of sulfhydryl
groups in BSA. A higher degree of BSA thiolation by TR induces more profound alterations of its structure, resulting in minor
oligomerization and aggregation. A 50-fold molar excess of TR was found to be the optimal, balancing thiolation level and
adverse effect on protein structure. PCB was covalently attached to newly introduced sulfhydryl groups at pH 9 at 20-fold
PCB/BSA ratio. An increase in the TR/BSA molar ratio leads to increased efficiency of PCB conjugation with thiolated BSA. Compared
to native BSA, BSA–PCB conjugate binds quercetin with similar affinity but has higher antioxidant activity and increased
oxidative stability.
CONCLUSIONS: PCB-modified BSA could serve as a stable, food-compatible carrier of bioactive PCB, but also bind other ligands
that would be protected from oxidative damage due to the high antioxidant potential of covalently bound PCB. Thiolation by
TR is, at the same time, a simple method for the covalent functionalization of virtually any protein by bioactive PCB or for
obtaining PCB-based fluorescent probes.
PB  - Wiley
T2  - Journal of the Science of Food and Agriculture
T1  - Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties
DO  - 10.1002/jsfa.13649
ER  - 

@article{
author = "Radomirović, Mirjana and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2024",
abstract = "BACKGROUND: Phycocyanobilin (PCB) is an open-chain blue tetrapyrrole chromophore of C-phycocyanin (C-PC), a major chromoprotein
derived from the cyanobacterium Arthrospira platensis having numerous health-promoting effects. Relying on the
ability of PCB to attach to the sulfhydryl group of proteins, we propose a new method for covalent attachment of PCB to bovine
serum albumin (BSA) as a means of its functionalization.
RESULTS: Traut's reagent (TR, 2-iminothiolane), modifying lysine residues, was used to optimize the introduction of sulfhydryl
groups in BSA. A higher degree of BSA thiolation by TR induces more profound alterations of its structure, resulting in minor
oligomerization and aggregation. A 50-fold molar excess of TR was found to be the optimal, balancing thiolation level and
adverse effect on protein structure. PCB was covalently attached to newly introduced sulfhydryl groups at pH 9 at 20-fold
PCB/BSA ratio. An increase in the TR/BSA molar ratio leads to increased efficiency of PCB conjugation with thiolated BSA. Compared
to native BSA, BSA–PCB conjugate binds quercetin with similar affinity but has higher antioxidant activity and increased
oxidative stability.
CONCLUSIONS: PCB-modified BSA could serve as a stable, food-compatible carrier of bioactive PCB, but also bind other ligands
that would be protected from oxidative damage due to the high antioxidant potential of covalently bound PCB. Thiolation by
TR is, at the same time, a simple method for the covalent functionalization of virtually any protein by bioactive PCB or for
obtaining PCB-based fluorescent probes.",
publisher = "Wiley",
journal = "Journal of the Science of Food and Agriculture",
title = "Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties",
doi = "10.1002/jsfa.13649"
}

Radomirović, M., Gligorijević, N., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T.. (2024). Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties. in Journal of the Science of Food and Agriculture
Wiley..
https://doi.org/10.1002/jsfa.13649

Radomirović M, Gligorijević N, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties. in Journal of the Science of Food and Agriculture. 2024;.
doi:10.1002/jsfa.13649 .

Radomirović, Mirjana, Gligorijević, Nikola, Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković-Veličković, Tanja, "Fabrication and characterization of bovine serum albumin–phycocyanobilin conjugate: effect on antioxidant and ligand-binding properties" in Journal of the Science of Food and Agriculture (2024),
https://doi.org/10.1002/jsfa.13649 . .

TY  - JOUR
AU  - Mijatović, Aleksandar
AU  - Šeba, Tino
AU  - Gligorijević, Nevenka
AU  - Ćoćić, Dušan
AU  - Spasić, Snežana
AU  - Lolić, Aleksandar
AU  - Aranđelović, Sandra
AU  - Nikolić, Milan
AU  - Gabričević, Mario
AU  - Baošić, Rada
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7593
AB  - The molecular structures of six neutral copper(II) complexes with propylenediamine bridges and different terminal groups have been reported and evaluated. Different antioxidant tests were performed on these complexes. Additionally, the antibacterial and antifungal activities of the investigated compounds were assessed. The study was complemented with data on their interaction with human serum albumin (HSA) and evaluated using spectroscopic fluorescence techniques. The copper(II) complexes were found to bind to HSA at multiple sites (n = 0.82–1.72), displaying relatively high binding constants on the order of Ka = (4.8–8.8) × 104 M−1. Furthermore, binding constants calculated from microscale thermophoresis (MST) data were within the range of 1.27 × 104–1.13 × 105 M−1; these results correlated well with the above Ka values obtained by fluorimetry. Molecular docking simulations were employed to study the ability of the complexes to bind to target macromolecules, such as HSA and DNA. As a significant addition to understanding their biological behavior, an MTT assay was performed to investigate the cytotoxicity of the complexes. The antiproliferative activity of the investigated copper(II) complexes with propylenediamine ligands, along with cisplatin as a reference compound, was evaluated in two human cancer cell lines (LS-174 and MCF-7) and one normal cell line (MRC-5). The obtained results are discussed, providing the structure–activity relationship of the copper(II) complexes with Schiff base tetradentate ligands.
PB  - Royal Society of Chemistry
T2  - New Journal of Chemistry
T1  - Promising in vitro and in silico biological activity of tetradentate Schiff base copper(II) complexes with a propylenediamine bridge
VL  - 48
IS  - 13
SP  - 5959
DO  - 10.1039/D3NJ05270B
ER  - 

@article{
author = "Mijatović, Aleksandar and Šeba, Tino and Gligorijević, Nevenka and Ćoćić, Dušan and Spasić, Snežana and Lolić, Aleksandar and Aranđelović, Sandra and Nikolić, Milan and Gabričević, Mario and Baošić, Rada",
year = "2024",
abstract = "The molecular structures of six neutral copper(II) complexes with propylenediamine bridges and different terminal groups have been reported and evaluated. Different antioxidant tests were performed on these complexes. Additionally, the antibacterial and antifungal activities of the investigated compounds were assessed. The study was complemented with data on their interaction with human serum albumin (HSA) and evaluated using spectroscopic fluorescence techniques. The copper(II) complexes were found to bind to HSA at multiple sites (n = 0.82–1.72), displaying relatively high binding constants on the order of Ka = (4.8–8.8) × 104 M−1. Furthermore, binding constants calculated from microscale thermophoresis (MST) data were within the range of 1.27 × 104–1.13 × 105 M−1; these results correlated well with the above Ka values obtained by fluorimetry. Molecular docking simulations were employed to study the ability of the complexes to bind to target macromolecules, such as HSA and DNA. As a significant addition to understanding their biological behavior, an MTT assay was performed to investigate the cytotoxicity of the complexes. The antiproliferative activity of the investigated copper(II) complexes with propylenediamine ligands, along with cisplatin as a reference compound, was evaluated in two human cancer cell lines (LS-174 and MCF-7) and one normal cell line (MRC-5). The obtained results are discussed, providing the structure–activity relationship of the copper(II) complexes with Schiff base tetradentate ligands.",
publisher = "Royal Society of Chemistry",
journal = "New Journal of Chemistry",
title = "Promising in vitro and in silico biological activity of tetradentate Schiff base copper(II) complexes with a propylenediamine bridge",
volume = "48",
number = "13",
pages = "5959",
doi = "10.1039/D3NJ05270B"
}

Mijatović, A., Šeba, T., Gligorijević, N., Ćoćić, D., Spasić, S., Lolić, A., Aranđelović, S., Nikolić, M., Gabričević, M.,& Baošić, R.. (2024). Promising in vitro and in silico biological activity of tetradentate Schiff base copper(II) complexes with a propylenediamine bridge. in New Journal of Chemistry
Royal Society of Chemistry., 48(13), 5959.
https://doi.org/10.1039/D3NJ05270B

Mijatović A, Šeba T, Gligorijević N, Ćoćić D, Spasić S, Lolić A, Aranđelović S, Nikolić M, Gabričević M, Baošić R. Promising in vitro and in silico biological activity of tetradentate Schiff base copper(II) complexes with a propylenediamine bridge. in New Journal of Chemistry. 2024;48(13):5959.
doi:10.1039/D3NJ05270B .

Mijatović, Aleksandar, Šeba, Tino, Gligorijević, Nevenka, Ćoćić, Dušan, Spasić, Snežana, Lolić, Aleksandar, Aranđelović, Sandra, Nikolić, Milan, Gabričević, Mario, Baošić, Rada, "Promising in vitro and in silico biological activity of tetradentate Schiff base copper(II) complexes with a propylenediamine bridge" in New Journal of Chemistry, 48, no. 13 (2024):5959,
https://doi.org/10.1039/D3NJ05270B . .

TY  - CONF
AU  - Tubić, Lora
AU  - Dragić, Milorad
AU  - Nikolić, Marija S.
AU  - Nikolić, Milan
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
PY  - 2024
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7690
AB  - Hydrogels play a significant role in the food industry as three-dimensional polymer networks.
Hydrogels have found extensive use not only in the production of traditional food products but also
in designing carriers for bioactive components. Developing hydrogels for food applications
prioritizes the use of natural ingredients and simple production methods. Extracts from the red
microalgae Porphyridium purpureum contain sulphated polysaccharides and vibrantly coloured
phycobiliproteins (PBPs), notably B-Phycoerythrin. This makes Porphyridium purpureum an
excellent starting point for developing food-based hydrogels with strong bioactive properties. This
work aims to develop and characterize the hydrogels from water extracts of Porphyridium
purpureum. In order to achieve that, we used the gelling property of the extract under acidic
conditions at pH 2.0. Two types of hydrogels based on this algal extract were compared. The first is
formed solely in an acidic environment, while the second is formed by adding alginate at the same
pH in the presence of calcium ions. The mechanical properties of both hydrogels were determined
by frequency sweep measurements using a rheometer with applied plane/plane geometry.
Rheological measurements showed that adding alginate significantly increases the mechanical
properties and elasticity of the hydrogel. Confocal microscopy demonstrated stronger fluorescence
of PBPs in the gel without alginate. Furthermore, the distribution of different PBPs within the gel
network is more uniform without alginate. The digestibility of the hydrogels was evaluated using an
in vitro static digestion model. Although both hydrogels were confirmed to be digestible, the
hydrogel without adding alginate showed higher digestibility. Antioxidant assays, ABTS and a
reducing power test showed that bioaccessible peptides after digestion of both hydrogels possess
antioxidant activity, with those obtained without alginate having a higher activity. Overall, this
research provides a simple and effective approach for developing coloured hydrogels with attractive
appearance, good bioaccessibility and notable bioactive properties.
PB  - Faculty of Agriculture
C3  - UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia
T1  - Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate
SP  - 164
EP  - 164
UR  - https://hdl.handle.net/21.15107/rcub_cer_7690
ER  - 

@conference{
author = "Tubić, Lora and Dragić, Milorad and Nikolić, Marija S. and Nikolić, Milan and Gligorijević, Nikola and Minić, Simeon",
year = "2024",
abstract = "Hydrogels play a significant role in the food industry as three-dimensional polymer networks.
Hydrogels have found extensive use not only in the production of traditional food products but also
in designing carriers for bioactive components. Developing hydrogels for food applications
prioritizes the use of natural ingredients and simple production methods. Extracts from the red
microalgae Porphyridium purpureum contain sulphated polysaccharides and vibrantly coloured
phycobiliproteins (PBPs), notably B-Phycoerythrin. This makes Porphyridium purpureum an
excellent starting point for developing food-based hydrogels with strong bioactive properties. This
work aims to develop and characterize the hydrogels from water extracts of Porphyridium
purpureum. In order to achieve that, we used the gelling property of the extract under acidic
conditions at pH 2.0. Two types of hydrogels based on this algal extract were compared. The first is
formed solely in an acidic environment, while the second is formed by adding alginate at the same
pH in the presence of calcium ions. The mechanical properties of both hydrogels were determined
by frequency sweep measurements using a rheometer with applied plane/plane geometry.
Rheological measurements showed that adding alginate significantly increases the mechanical
properties and elasticity of the hydrogel. Confocal microscopy demonstrated stronger fluorescence
of PBPs in the gel without alginate. Furthermore, the distribution of different PBPs within the gel
network is more uniform without alginate. The digestibility of the hydrogels was evaluated using an
in vitro static digestion model. Although both hydrogels were confirmed to be digestible, the
hydrogel without adding alginate showed higher digestibility. Antioxidant assays, ABTS and a
reducing power test showed that bioaccessible peptides after digestion of both hydrogels possess
antioxidant activity, with those obtained without alginate having a higher activity. Overall, this
research provides a simple and effective approach for developing coloured hydrogels with attractive
appearance, good bioaccessibility and notable bioactive properties.",
publisher = "Faculty of Agriculture",
journal = "UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia",
title = "Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate",
pages = "164-164",
url = "https://hdl.handle.net/21.15107/rcub_cer_7690"
}

Tubić, L., Dragić, M., Nikolić, M. S., Nikolić, M., Gligorijević, N.,& Minić, S.. (2024). Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate. in UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia
Faculty of Agriculture., 164-164.
https://hdl.handle.net/21.15107/rcub_cer_7690

Tubić L, Dragić M, Nikolić MS, Nikolić M, Gligorijević N, Minić S. Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate. in UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia. 2024;:164-164.
https://hdl.handle.net/21.15107/rcub_cer_7690 .

Tubić, Lora, Dragić, Milorad, Nikolić, Marija S., Nikolić, Milan, Gligorijević, Nikola, Minić, Simeon, "Composite hydrogels obtained from extracts of Porphyridium purpureum and alginate" in UNIFood2024 Conference, 3rd International UNIfood Conference, Book of Abstracts, June 28-29, 2024, Belgrade, Serbia (2024):164-164,
https://hdl.handle.net/21.15107/rcub_cer_7690 .

TY  - CONF
AU  - Jovanović, Zorana
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Pavlović, Vladimir B.
AU  - Lević, Steva
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7521
AB  - Our study aimed to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae due to its importance in the food industry. We
incorporated C-PC into hydrogels formed by combining starch and β-lactoglobulin (BLG)
using high-pressure (HP) processing to achieve this objective. Notably, thermal treatment
resulted in the complete loss of colour derived from C-PC.
We performed a comprehensive characterization of the resulting HP gels by rheology
measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and
scanning electron microscopy (SEM).
Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The
C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7,
maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations
of components were retained in the binary systems.
Rheological properties of the gels were determined using a rheometer with
plane/plane geometry, and texture analysis was conducted through TPA. These findings
enabled the assessment of food gel's properties, such as hardness, springiness, chewiness, and
cohesiveness. The structural characteristics of the gels were determined by SAXS, offering
insights into the interactions between C-PC, BLG, and starch after HP processing. Adding CPC
and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the
gel surface revealed that all components influenced the overall morphology of gels. Even at
low concentrations, the addition of starch notably influenced the gels' visual appearance and
mechanical properties. Our investigation highlights the superior effectiveness of HP treatment
in the preservation of C-PC compared to high-temperature treatment, evident in the sustained
colour integrity of the C-PC blue dye.
PB  - Faculty of Technology and Metallurgy, University of Belgrade
C3  - Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade
T1  - The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin
SP  - 60
EP  - 60
UR  - https://hdl.handle.net/21.15107/rcub_cer_7521
ER  - 

@conference{
author = "Jovanović, Zorana and Annighöfer, Burkhard and Dudzinski, Daniel and Gligorijević, Nikola and Nikolić, Milan and Pavlović, Vladimir B. and Lević, Steva and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2023",
abstract = "Our study aimed to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae due to its importance in the food industry. We
incorporated C-PC into hydrogels formed by combining starch and β-lactoglobulin (BLG)
using high-pressure (HP) processing to achieve this objective. Notably, thermal treatment
resulted in the complete loss of colour derived from C-PC.
We performed a comprehensive characterization of the resulting HP gels by rheology
measurements, texture profile analysis (TPA), small-angle X-ray scattering (SAXS), and
scanning electron microscopy (SEM).
Different compositions of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were processed under high-pressure (HP) conditions reaching up to 4,500 bar. The
C-PC pigment was effectively preserved by mixing BLG and starch with C-PC at pH 7,
maintaining concentrations of 180, 5, and 10 mg/mL, respectively. The same concentrations
of components were retained in the binary systems.
Rheological properties of the gels were determined using a rheometer with
plane/plane geometry, and texture analysis was conducted through TPA. These findings
enabled the assessment of food gel's properties, such as hardness, springiness, chewiness, and
cohesiveness. The structural characteristics of the gels were determined by SAXS, offering
insights into the interactions between C-PC, BLG, and starch after HP processing. Adding CPC
and starch formed solid gels with a larger mesh than the pure BLG gels. SEM scans of the
gel surface revealed that all components influenced the overall morphology of gels. Even at
low concentrations, the addition of starch notably influenced the gels' visual appearance and
mechanical properties. Our investigation highlights the superior effectiveness of HP treatment
in the preservation of C-PC compared to high-temperature treatment, evident in the sustained
colour integrity of the C-PC blue dye.",
publisher = "Faculty of Technology and Metallurgy, University of Belgrade",
journal = "Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade",
title = "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin",
pages = "60-60",
url = "https://hdl.handle.net/21.15107/rcub_cer_7521"
}

Jovanović, Z., Annighöfer, B., Dudzinski, D., Gligorijević, N., Nikolić, M., Pavlović, V. B., Lević, S., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2023). The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade
Faculty of Technology and Metallurgy, University of Belgrade., 60-60.
https://hdl.handle.net/21.15107/rcub_cer_7521

Jovanović Z, Annighöfer B, Dudzinski D, Gligorijević N, Nikolić M, Pavlović VB, Lević S, Brûlet A, Assifaoui A, Combet S, Minić S. The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin. in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade. 2023;:60-60.
https://hdl.handle.net/21.15107/rcub_cer_7521 .

Jovanović, Zorana, Annighöfer, Burkhard, Dudzinski, Daniel, Gligorijević, Nikola, Nikolić, Milan, Pavlović, Vladimir B., Lević, Steva, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "The use of starch and β-lactoglobulin composite hydrogels as frameworks for preserving c-phycocyanin" in Book of abstracts - International Conference on Biochemical Engineering and Biotechnology for Young Scientists, Belgrade (2023):60-60,
https://hdl.handle.net/21.15107/rcub_cer_7521 .

TY  - JOUR
AU  - Mijatović, Aleksandar
AU  - Gligorijević, Nevenka
AU  - Ćoćić, Dušan
AU  - Spasić, Snežana
AU  - Lolić, Aleksandar
AU  - Aranđelović, Sandra
AU  - Nikolić, Milan
AU  - Baošić, Rada
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6777
AB  - The biological activity of six structurally similar tetradentate Schiff base copper(II) complexes, namely [Cu(ethylenediamine-bis-acetylacetonate)] (CuAA) and five derivatives where two methyl groups are replaced by phenyl, (CuPP), CF3 (CuTT) or by mixed groups CH3/CF3 (CuAT), Ph/CF3 (CuPT), and Ph/CH3 (CuAP) has been investigated. The set of antioxidant assays was performed, and the results were expressed as IC50 and EC50 values. The series of complexes showed interesting bioactivity and were investigated for the determination of antioxidant, antifungal, antimicrobial, and cytotoxic activity. A significant antioxidant behavior was exhibited by complex CuAA, greater than Trolox in the Oxygen Radical Absorbance Capacity (ORAC) assay. Antibacterial assay over Gram-positive and Gram-negative pathogenic bacterial strains and some fungal pathogens were studied. Antiproliferative activity of complexes in two human tumor cell lines, breast adenocarcinoma MCF-7, colon adenocarcinoma LS-174, and normal fibroblast cells-MRC-5, examined the effect on cell cycle progression. The significant cytotoxic potential, comparable to cisplatin cytotoxicity, was determined in human breast cancer cell line-MCF-7 with IC50 values being 17.53–31.40 μM and human colon cancer cell line-LS-174 with IC50 values being 15.22–23.92 μM. All tested compounds showed nearly twice more selectivity toward cancer cell lines than normal cells. The interactions of complexes with human serum albumin (HSA), the most prominent protein in plasma, were investigated using spectroscopic fluorescence techniques. The complexes bind to human serum albumin at multiple sites (n = 0.2–1.9), displaying a moderate binding constant Ka = 4.1–12.4 × 104 M−1. The molecular docking experiment effectively showed complex binding to HSA and DNA molecular fragments.
PB  - Elsevier
T2  - Journal of Inorganic Biochemistry
T1  - In vitro and in silico study of the biological activity of tetradentate Schiff base copper(II) complexes with ethylenediamine-bridge
VL  - 244
SP  - 112224
DO  - 10.1016/j.jinorgbio.2023.112224
ER  - 

@article{
author = "Mijatović, Aleksandar and Gligorijević, Nevenka and Ćoćić, Dušan and Spasić, Snežana and Lolić, Aleksandar and Aranđelović, Sandra and Nikolić, Milan and Baošić, Rada",
year = "2023",
abstract = "The biological activity of six structurally similar tetradentate Schiff base copper(II) complexes, namely [Cu(ethylenediamine-bis-acetylacetonate)] (CuAA) and five derivatives where two methyl groups are replaced by phenyl, (CuPP), CF3 (CuTT) or by mixed groups CH3/CF3 (CuAT), Ph/CF3 (CuPT), and Ph/CH3 (CuAP) has been investigated. The set of antioxidant assays was performed, and the results were expressed as IC50 and EC50 values. The series of complexes showed interesting bioactivity and were investigated for the determination of antioxidant, antifungal, antimicrobial, and cytotoxic activity. A significant antioxidant behavior was exhibited by complex CuAA, greater than Trolox in the Oxygen Radical Absorbance Capacity (ORAC) assay. Antibacterial assay over Gram-positive and Gram-negative pathogenic bacterial strains and some fungal pathogens were studied. Antiproliferative activity of complexes in two human tumor cell lines, breast adenocarcinoma MCF-7, colon adenocarcinoma LS-174, and normal fibroblast cells-MRC-5, examined the effect on cell cycle progression. The significant cytotoxic potential, comparable to cisplatin cytotoxicity, was determined in human breast cancer cell line-MCF-7 with IC50 values being 17.53–31.40 μM and human colon cancer cell line-LS-174 with IC50 values being 15.22–23.92 μM. All tested compounds showed nearly twice more selectivity toward cancer cell lines than normal cells. The interactions of complexes with human serum albumin (HSA), the most prominent protein in plasma, were investigated using spectroscopic fluorescence techniques. The complexes bind to human serum albumin at multiple sites (n = 0.2–1.9), displaying a moderate binding constant Ka = 4.1–12.4 × 104 M−1. The molecular docking experiment effectively showed complex binding to HSA and DNA molecular fragments.",
publisher = "Elsevier",
journal = "Journal of Inorganic Biochemistry",
title = "In vitro and in silico study of the biological activity of tetradentate Schiff base copper(II) complexes with ethylenediamine-bridge",
volume = "244",
pages = "112224",
doi = "10.1016/j.jinorgbio.2023.112224"
}

Mijatović, A., Gligorijević, N., Ćoćić, D., Spasić, S., Lolić, A., Aranđelović, S., Nikolić, M.,& Baošić, R.. (2023). In vitro and in silico study of the biological activity of tetradentate Schiff base copper(II) complexes with ethylenediamine-bridge. in Journal of Inorganic Biochemistry
Elsevier., 244, 112224.
https://doi.org/10.1016/j.jinorgbio.2023.112224

Mijatović A, Gligorijević N, Ćoćić D, Spasić S, Lolić A, Aranđelović S, Nikolić M, Baošić R. In vitro and in silico study of the biological activity of tetradentate Schiff base copper(II) complexes with ethylenediamine-bridge. in Journal of Inorganic Biochemistry. 2023;244:112224.
doi:10.1016/j.jinorgbio.2023.112224 .

Mijatović, Aleksandar, Gligorijević, Nevenka, Ćoćić, Dušan, Spasić, Snežana, Lolić, Aleksandar, Aranđelović, Sandra, Nikolić, Milan, Baošić, Rada, "In vitro and in silico study of the biological activity of tetradentate Schiff base copper(II) complexes with ethylenediamine-bridge" in Journal of Inorganic Biochemistry, 244 (2023):112224,
https://doi.org/10.1016/j.jinorgbio.2023.112224 . .

TY  - JOUR
AU  - Breberina, Luka
AU  - Nikolić, Milan
AU  - Stojanović, Srđan
AU  - Zlatović, Mario
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6502
AB  - The influences of π−π interactions in phycocyanin proteins and their
environmental preferences were analyzed. The observations indicate that the
majority of the aromatic residues in phycocyanin proteins are involved in π−π
interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be
involved in π–π interactions much more frequently than tryptophan (Trp) or
histidine (His). Similarly, the Phe−Phe and Tyr−Tyr π–π interacting pair had
the highest frequency of occurrence. In addition to π-π interactions, the aromatic
residues also form π-networks in phycocyanins. The π–π interactions are
most favourable at the pair distance range of 5.5–7 Å, with a clear preference
for T-shaped ring arrangements. Using ab initio calculations, we observed that
most of the π−π interactions possess energy from 0 to −10 kJ mol-1. Stabilization
centres for these proteins showed that all residues found in π−π interactions
are important in locating one or more such centres. π−π interacting residues
are evolutionary conserved. The results obtained from this study will be
beneficial in further understanding the structural stability and eventual development
of protein engineering of phycocyanins.
AB  - Анализирани су утицаји π−π интеракција у протеинима фикоцијанинима и њихове
преференције ка окружењу. Запажања показују да је већина ароматичних остатака у
протеинима фикоцијанинима укључена у π−π интеракције. Утврђено је да су остаци фенилаланина (Phe) и тирозина (Tyr) много чешће укључени у π–π интеракције него триптофана (Trp) или хистидина (His). Слично томе, интерагујући π–π парови Phe−Phe и Tyr−Tyr имали су највећу учесталост појављивања. Додатно, ароматични остаци такође
стварају π-мреже у фикоцијанинима. π–π интеракције су најповољније у распону дистанци парова од 5,5–7 Å, с јасном склоношћу за распоред прстенова у облику слова Т. Користећи ab initio прорачуне, приметили смо да већина π−π интеракција има енергију у распону од 0 до −10 kJ mol-1. Стабилизациони центри ових протеина показали су да су сви остаци пронађени у π−π интеракцијама важни у лоцирању једног или више таквих центара. π−π интеракциони остаци су еволутивно конзервирани. Резултати добивени овом студијом биће од користи у даљем разумевању структурне стабилности и евентуалном развоју протеинског инжењеринга фикоцијанина.
PB  - Belgrade : Serbian Chemical Society
T2  - Journal of the Serbian Chemical Society
T1  - On the importance of π–π interactions in structural stability of phycocyanins
T1  - О значају π−π интеракција у структурној стабилности фикоцијанина
VL  - 88
IS  - 5
SP  - 481
EP  - 494
DO  - 10.2298/JSC221201008B
ER  - 

@article{
author = "Breberina, Luka and Nikolić, Milan and Stojanović, Srđan and Zlatović, Mario",
year = "2023",
abstract = "The influences of π−π interactions in phycocyanin proteins and their
environmental preferences were analyzed. The observations indicate that the
majority of the aromatic residues in phycocyanin proteins are involved in π−π
interactions. Phenylalanine (Phe) and tyrosine (Tyr) residues were found to be
involved in π–π interactions much more frequently than tryptophan (Trp) or
histidine (His). Similarly, the Phe−Phe and Tyr−Tyr π–π interacting pair had
the highest frequency of occurrence. In addition to π-π interactions, the aromatic
residues also form π-networks in phycocyanins. The π–π interactions are
most favourable at the pair distance range of 5.5–7 Å, with a clear preference
for T-shaped ring arrangements. Using ab initio calculations, we observed that
most of the π−π interactions possess energy from 0 to −10 kJ mol-1. Stabilization
centres for these proteins showed that all residues found in π−π interactions
are important in locating one or more such centres. π−π interacting residues
are evolutionary conserved. The results obtained from this study will be
beneficial in further understanding the structural stability and eventual development
of protein engineering of phycocyanins., Анализирани су утицаји π−π интеракција у протеинима фикоцијанинима и њихове
преференције ка окружењу. Запажања показују да је већина ароматичних остатака у
протеинима фикоцијанинима укључена у π−π интеракције. Утврђено је да су остаци фенилаланина (Phe) и тирозина (Tyr) много чешће укључени у π–π интеракције него триптофана (Trp) или хистидина (His). Слично томе, интерагујући π–π парови Phe−Phe и Tyr−Tyr имали су највећу учесталост појављивања. Додатно, ароматични остаци такође
стварају π-мреже у фикоцијанинима. π–π интеракције су најповољније у распону дистанци парова од 5,5–7 Å, с јасном склоношћу за распоред прстенова у облику слова Т. Користећи ab initio прорачуне, приметили смо да већина π−π интеракција има енергију у распону од 0 до −10 kJ mol-1. Стабилизациони центри ових протеина показали су да су сви остаци пронађени у π−π интеракцијама важни у лоцирању једног или више таквих центара. π−π интеракциони остаци су еволутивно конзервирани. Резултати добивени овом студијом биће од користи у даљем разумевању структурне стабилности и евентуалном развоју протеинског инжењеринга фикоцијанина.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Journal of the Serbian Chemical Society",
title = "On the importance of π–π interactions in structural stability of phycocyanins, О значају π−π интеракција у структурној стабилности фикоцијанина",
volume = "88",
number = "5",
pages = "481-494",
doi = "10.2298/JSC221201008B"
}

Breberina, L., Nikolić, M., Stojanović, S.,& Zlatović, M.. (2023). On the importance of π–π interactions in structural stability of phycocyanins. in Journal of the Serbian Chemical Society
Belgrade : Serbian Chemical Society., 88(5), 481-494.
https://doi.org/10.2298/JSC221201008B

Breberina L, Nikolić M, Stojanović S, Zlatović M. On the importance of π–π interactions in structural stability of phycocyanins. in Journal of the Serbian Chemical Society. 2023;88(5):481-494.
doi:10.2298/JSC221201008B .

Breberina, Luka, Nikolić, Milan, Stojanović, Srđan, Zlatović, Mario, "On the importance of π–π interactions in structural stability of phycocyanins" in Journal of the Serbian Chemical Society, 88, no. 5 (2023):481-494,
https://doi.org/10.2298/JSC221201008B . .

TY  - JOUR
AU  - Nedić, Olgica
AU  - Penezić, Ana
AU  - Minić, Simeon
AU  - Radomirović, Mirjana
AU  - Nikolić, Milan
AU  - Ćirković Veličković, Tanja
AU  - Gligorijević, Nikola
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6485
AB  - Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Antioxidants
T1  - Food Antioxidants and Their Interaction with Human Proteins
VL  - 12
IS  - 4
SP  - 815
DO  - 10.3390/antiox12040815
ER  - 

@article{
author = "Nedić, Olgica and Penezić, Ana and Minić, Simeon and Radomirović, Mirjana and Nikolić, Milan and Ćirković Veličković, Tanja and Gligorijević, Nikola",
year = "2023",
abstract = "Common to all biological systems and living organisms are molecular interactions, which
may lead to specific physiological events. Most often, a cascade of events occurs, establishing an
equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that
sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases.
This article deals with food antioxidants and human proteins from the circulation, their interaction,
their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible
impact of complex formation on antioxidants. An overview of studies examining interactions between
individual antioxidant compounds and major blood proteins is presented with findings. Investigating
antioxidant/protein interactions at the level of the human organism and determining antioxidant
distribution between proteins and involvement in the particular physiological role is a very complex
and challenging task. However, by knowing the role of a particular protein in certain pathology or
aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend
specific food intake or resistance to it to improve the condition or slow down the process.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Antioxidants",
title = "Food Antioxidants and Their Interaction with Human Proteins",
volume = "12",
number = "4",
pages = "815",
doi = "10.3390/antiox12040815"
}

Nedić, O., Penezić, A., Minić, S., Radomirović, M., Nikolić, M., Ćirković Veličković, T.,& Gligorijević, N.. (2023). Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants
Multidisciplinary Digital Publishing Institute (MDPI)., 12(4), 815.
https://doi.org/10.3390/antiox12040815

Nedić O, Penezić A, Minić S, Radomirović M, Nikolić M, Ćirković Veličković T, Gligorijević N. Food Antioxidants and Their Interaction with Human Proteins. in Antioxidants. 2023;12(4):815.
doi:10.3390/antiox12040815 .

Nedić, Olgica, Penezić, Ana, Minić, Simeon, Radomirović, Mirjana, Nikolić, Milan, Ćirković Veličković, Tanja, Gligorijević, Nikola, "Food Antioxidants and Their Interaction with Human Proteins" in Antioxidants, 12, no. 4 (2023):815,
https://doi.org/10.3390/antiox12040815 . .

TY  - JOUR
AU  - Platanić Arizanović, Lena
AU  - Gligorijević, Nikola
AU  - Cvijetić, Ilija
AU  - Mijatović, Aleksandar
AU  - Krstić Ristivojević, Maja
AU  - Minić, Simeon
AU  - Nikolić Kokić, Aleksandra
AU  - Miljević, Čedo
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6482
AB  - Packed with hemoglobin, an essential protein for oxygen transport, human erythrocytes
are a suitable model system for testing the pleiotropic effects of lipophilic drugs. Our study investigated the interaction between antipsychotic drugs clozapine, ziprasidone, sertindole, and human hemoglobin under simulated physiological conditions. Analysis of protein fluorescence quenching at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ  interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~10^4 M^-1), the highest observed for clozapine (2.2 x 10^4 M^-1 at 25 °C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - International Journal of Molecular Sciences
T1  - Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?
VL  - 24
IS  - 10
SP  - 8921
DO  - 10.3390/ijms24108921
ER  - 

@article{
author = "Platanić Arizanović, Lena and Gligorijević, Nikola and Cvijetić, Ilija and Mijatović, Aleksandar and Krstić Ristivojević, Maja and Minić, Simeon and Nikolić Kokić, Aleksandra and Miljević, Čedo and Nikolić, Milan",
year = "2023",
abstract = "Packed with hemoglobin, an essential protein for oxygen transport, human erythrocytes
are a suitable model system for testing the pleiotropic effects of lipophilic drugs. Our study investigated the interaction between antipsychotic drugs clozapine, ziprasidone, sertindole, and human hemoglobin under simulated physiological conditions. Analysis of protein fluorescence quenching at different temperatures and data obtained from the van’t Hoff diagram and molecular docking indicate that the interactions are static and that the tetrameric human hemoglobin has one binding site for all drugs in the central cavity near αβ  interfaces and is dominantly mediated through hydrophobic forces. The association constants were lower-moderate strength (~10^4 M^-1), the highest observed for clozapine (2.2 x 10^4 M^-1 at 25 °C). The clozapine binding showed “friendly” effects: increased α-helical content, a higher melting point, and protein protection from free radical-mediated oxidation. On the other hand, bound ziprasidone and sertindole had a slightly pro-oxidative effect, increasing ferrihemoglobin content, a possible “foe”. Since the interaction of proteins with drugs plays a vital role in their pharmacokinetic and pharmacodynamic properties, the physiological significance of the obtained findings is briefly discussed.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "International Journal of Molecular Sciences",
title = "Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?",
volume = "24",
number = "10",
pages = "8921",
doi = "10.3390/ijms24108921"
}

Platanić Arizanović, L., Gligorijević, N., Cvijetić, I., Mijatović, A., Krstić Ristivojević, M., Minić, S., Nikolić Kokić, A., Miljević, Č.,& Nikolić, M.. (2023). Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?. in International Journal of Molecular Sciences
Multidisciplinary Digital Publishing Institute (MDPI)., 24(10), 8921.
https://doi.org/10.3390/ijms24108921

Platanić Arizanović L, Gligorijević N, Cvijetić I, Mijatović A, Krstić Ristivojević M, Minić S, Nikolić Kokić A, Miljević Č, Nikolić M. Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?. in International Journal of Molecular Sciences. 2023;24(10):8921.
doi:10.3390/ijms24108921 .

Platanić Arizanović, Lena, Gligorijević, Nikola, Cvijetić, Ilija, Mijatović, Aleksandar, Krstić Ristivojević, Maja, Minić, Simeon, Nikolić Kokić, Aleksandra, Miljević, Čedo, Nikolić, Milan, "Human Hemoglobin and Antipsychotics Clozapine, Ziprasidone and Sertindole: Friends or Foes?" in International Journal of Molecular Sciences, 24, no. 10 (2023):8921,
https://doi.org/10.3390/ijms24108921 . .

TY  - JOUR
AU  - Šunderić, Miloš
AU  - Gligorijević, Nikola
AU  - Milčić, Miloš
AU  - Minić, Simeon
AU  - Nedić, Olgica
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6471
AB  - Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.
PB  - Taylor & Francis Group
T2  - Journal of Biomolecular Structure and Dynamics
T1  - Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress
DO  - 10.1080/07391102.2023.2248273
ER  - 

@article{
author = "Šunderić, Miloš and Gligorijević, Nikola and Milčić, Miloš and Minić, Simeon and Nedić, Olgica and Nikolić, Milan",
year = "2023",
abstract = "Under simulated physiological conditions, this study investigates the interaction between nutraceutical phycocyanobilin (PCB) and the universal anti-protease protein human alpha-2-macroglobulin (a2M). Extensive molecular docking analyses on multiple a2M conformations, spectroscopic techniques, and a2M activity assays were utilized to examine the complex formation. The results revealed that for every protein conformation, two high energy binding sites exist: the first, conformationally independent, at the interface region between two monomer chains and the second, conformationally dependent, in the pocket composed of amino acids from four distinct domains (TED, RBD, CUB, and MG2) of the single protein chain. Spectrofluorimetric measurements indicated a moderate affinity between a2M and PCB with a moderately high binding constant of 6.3 x 10^5 M^-1 at 25 °C. The binding of PCB to a2M resulted in minor changes in the secondary structure content of a2M. Furthermore, PCB protected a2M from oxidation and preserved its anti-protease activity in the oxidative environment. These findings suggest that PCB binding could indirectly impact the body’s response to oxidative stress by influencing a2M’s role in controlling enzyme activity during the inflammatory process.",
publisher = "Taylor & Francis Group",
journal = "Journal of Biomolecular Structure and Dynamics",
title = "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress",
doi = "10.1080/07391102.2023.2248273"
}

Šunderić, M., Gligorijević, N., Milčić, M., Minić, S., Nedić, O.,& Nikolić, M.. (2023). Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics
Taylor & Francis Group..
https://doi.org/10.1080/07391102.2023.2248273

Šunderić M, Gligorijević N, Milčić M, Minić S, Nedić O, Nikolić M. Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress. in Journal of Biomolecular Structure and Dynamics. 2023;.
doi:10.1080/07391102.2023.2248273 .

Šunderić, Miloš, Gligorijević, Nikola, Milčić, Miloš, Minić, Simeon, Nedić, Olgica, Nikolić, Milan, "Phycocyanobilin is a new binding partner of human alpha-2-macroglobulin that protects the protein against oxidative stress" in Journal of Biomolecular Structure and Dynamics (2023),
https://doi.org/10.1080/07391102.2023.2248273 . .

TY  - JOUR
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Thureau, Aurelien
AU  - Obradović, Milica
AU  - Vasović, Tamara
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Brulet, Annie
AU  - Ćirković Veličković, Tanja
AU  - Combet, Sophie
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6473
AB  - This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on RPC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual
capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.
PB  - Elsevier Ltd.
T2  - Food Chemistry
T1  - Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant
VL  - 426
SP  - 136669
DO  - 10.1016/j.foodchem.2023.136669
ER  - 

@article{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Thureau, Aurelien and Obradović, Milica and Vasović, Tamara and Sotiroudis, Georgios and Zoumpanioti, Maria and Brulet, Annie and Ćirković Veličković, Tanja and Combet, Sophie and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "This study aimed to purify, characterise and stabilise the natural food colourant, R-phycocyanin (R-PC), from the red algae Porphyra spp. (Nori). We purified R-PC from dried Nori flakes with a high purity ratio (A618/A280 ≥ 3.4) in native form (α-helix content 53%). SAXS measurements revealed that R-PC is trimeric ((αβ)3) in solution. The thermal denaturation of α-helix revealed one transition (Tm at 52 ◦C), while the pH stability study showed R-PC is stable in the pH range 4–8. The thermal treatment of R-PC at 60 °C has detrimental and irreversible effects on RPC colour and antioxidant capacity (22 % of residual capacity). However, immobilisation of R-PC within calcium alginate beads completely preserves R-PC colour and mainly retains its antioxidant ability (78 % of residual
capacity). Results give new insights into the stability of R-PC and preservation of its purple colour and bioactivity by encapsulation in calcium alginate beads.",
publisher = "Elsevier Ltd.",
journal = "Food Chemistry",
title = "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant",
volume = "426",
pages = "136669",
doi = "10.1016/j.foodchem.2023.136669"
}

Veličković, L., Simović, A., Gligorijević, N., Thureau, A., Obradović, M., Vasović, T., Sotiroudis, G., Zoumpanioti, M., Brulet, A., Ćirković Veličković, T., Combet, S., Nikolić, M.,& Minić, S.. (2023). Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry
Elsevier Ltd.., 426, 136669.
https://doi.org/10.1016/j.foodchem.2023.136669

Veličković L, Simović A, Gligorijević N, Thureau A, Obradović M, Vasović T, Sotiroudis G, Zoumpanioti M, Brulet A, Ćirković Veličković T, Combet S, Nikolić M, Minić S. Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant. in Food Chemistry. 2023;426:136669.
doi:10.1016/j.foodchem.2023.136669 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Thureau, Aurelien, Obradović, Milica, Vasović, Tamara, Sotiroudis, Georgios, Zoumpanioti, Maria, Brulet, Annie, Ćirković Veličković, Tanja, Combet, Sophie, Nikolić, Milan, Minić, Simeon, "Exploring and strengthening the potential of R-phycocyanin from Nori flakes as a food colourant" in Food Chemistry, 426 (2023):136669,
https://doi.org/10.1016/j.foodchem.2023.136669 . .

TY  - CONF
AU  - Veličković, Luka
AU  - Simović, Ana
AU  - Gligorijević, Nikola
AU  - Obradović, Milica
AU  - Sotiroudis, Georgios
AU  - Zoumpanioti, Maria
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6505
AB  - Purple R-phycocyanin is a protein from red algae with the potential for application in the food industry (colorant) and wastewater treatment (binding of heavy metals). Analytical grade R-phycocyanin was purified from the buffered extract of dried Nori flakes (Porphyra spp.) by combining ammonium sulfate precipitation, hydroxyapatite, and DEAE-Sepharose column chromatography. The multimeric protein had absorption maxima characteristic for phycoerythrobilin (at 580 nm) and phycocyanobilin (at 640 nm) chromophores, high α- helical content, and melting temperature of 52°C. The secondary R-PC structure was stable under a wide range of pH values (3–9). R-phycocyanin immobilized in calcium alginate beads showed increased thermal stability and preserved antioxidant activity.
AB  - Ljubičasti R-fikocijanin je protein crvenih algi sa mogućnostima primene u industriji hrane (kolorant) i za tretman otpadnih voda (vezuje teške metale). R-fikocijanin analitičke čistoće je izolovan iz puferisanog ekstrakta osušenih Nori algi (Porphyra spp.), kombinacijom taloženja amonijum-sulfatom, hidroksiapatitne i hromatografije na DEAE-Sepharose koloni. Multimerni protein imao je apsorpcione maksimume karakteristične za fikoeritrobilinsku (na 580 nm) i fikocijanobilinsku (na 640 nm) hromoforu, visok sadržaj α-zavojnica i temperaturu topljenja od 52°C. Sekundarna struktura proteina bila je stabilna u širokom rasponu pH vrednosti (3–9). R-fikocijanin imobilisan u kuglice kalcijum-alginata pokazao je povećanu toplotnu stabilnost i očuvana antioksidativna svojstva.
PB  - Belgrade : Serbian Chemical Society
C3  - Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia
T1  - Purification and structural characterization of R-phycocyanin
T1  - Prečišćavanje i strukturna karakterizacija R-fikocijanina
SP  - 53
EP  - 53
UR  - https://hdl.handle.net/21.15107/rcub_cer_6505
ER  - 

@conference{
author = "Veličković, Luka and Simović, Ana and Gligorijević, Nikola and Obradović, Milica and Sotiroudis, Georgios and Zoumpanioti, Maria and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "Purple R-phycocyanin is a protein from red algae with the potential for application in the food industry (colorant) and wastewater treatment (binding of heavy metals). Analytical grade R-phycocyanin was purified from the buffered extract of dried Nori flakes (Porphyra spp.) by combining ammonium sulfate precipitation, hydroxyapatite, and DEAE-Sepharose column chromatography. The multimeric protein had absorption maxima characteristic for phycoerythrobilin (at 580 nm) and phycocyanobilin (at 640 nm) chromophores, high α- helical content, and melting temperature of 52°C. The secondary R-PC structure was stable under a wide range of pH values (3–9). R-phycocyanin immobilized in calcium alginate beads showed increased thermal stability and preserved antioxidant activity., Ljubičasti R-fikocijanin je protein crvenih algi sa mogućnostima primene u industriji hrane (kolorant) i za tretman otpadnih voda (vezuje teške metale). R-fikocijanin analitičke čistoće je izolovan iz puferisanog ekstrakta osušenih Nori algi (Porphyra spp.), kombinacijom taloženja amonijum-sulfatom, hidroksiapatitne i hromatografije na DEAE-Sepharose koloni. Multimerni protein imao je apsorpcione maksimume karakteristične za fikoeritrobilinsku (na 580 nm) i fikocijanobilinsku (na 640 nm) hromoforu, visok sadržaj α-zavojnica i temperaturu topljenja od 52°C. Sekundarna struktura proteina bila je stabilna u širokom rasponu pH vrednosti (3–9). R-fikocijanin imobilisan u kuglice kalcijum-alginata pokazao je povećanu toplotnu stabilnost i očuvana antioksidativna svojstva.",
publisher = "Belgrade : Serbian Chemical Society",
journal = "Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia",
title = "Purification and structural characterization of R-phycocyanin, Prečišćavanje i strukturna karakterizacija R-fikocijanina",
pages = "53-53",
url = "https://hdl.handle.net/21.15107/rcub_cer_6505"
}

Veličković, L., Simović, A., Gligorijević, N., Obradović, M., Sotiroudis, G., Zoumpanioti, M., Minić, S.,& Nikolić, M.. (2023). Purification and structural characterization of R-phycocyanin. in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia
Belgrade : Serbian Chemical Society., 53-53.
https://hdl.handle.net/21.15107/rcub_cer_6505

Veličković L, Simović A, Gligorijević N, Obradović M, Sotiroudis G, Zoumpanioti M, Minić S, Nikolić M. Purification and structural characterization of R-phycocyanin. in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia. 2023;:53-53.
https://hdl.handle.net/21.15107/rcub_cer_6505 .

Veličković, Luka, Simović, Ana, Gligorijević, Nikola, Obradović, Milica, Sotiroudis, Georgios, Zoumpanioti, Maria, Minić, Simeon, Nikolić, Milan, "Purification and structural characterization of R-phycocyanin" in Kratki izvodi radova, knjiga radova - 59. Savetovanje Srpskog hemijskog društva, 1. i 2. jun 2023. godine, Novi Sad / Book of Abstracts, Proceedings - 59th Meeting of the Serbian Chemical Society, June 1-2, 2023, Novi Sad, Serbia (2023):53-53,
https://hdl.handle.net/21.15107/rcub_cer_6505 .

TY  - CONF
AU  - Gligorijević, Nikola
AU  - Veličković, Luka
AU  - Svrzić, Nikola
AU  - Jovanović, Zorana
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6519
AB  - C-Phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a phycobiliprotein with potent biological activity. It has several beneficial effects, including anti-oxidant, anti-inflammatory, immunomodulatory, and anti-cancer. A significant challenge for the broader application of C-PC in the food industry is its stability in food processing conditions, such
as increased light exposure, temperature, and high pressure and drying. This work aimed to investigate if the immobilization of C-PC onto alginate beads could improve its stability. C-PC was
immobilized by dropping the solution of C-PC and 1% alginate (final concentration) in the solution of 2% CaCl2. Both protein/alginate mixture and CaCl2 were kept at pH 4. Immobilized CPC
was treated for 30 min at 65°C, by high pressure up to 4500 bar, and incubated under light exposure for a month. Alginate beads with immobilized C-PC were also left to dry in the fridge and kept for a month. C-PC was extracted from alginate beads by immersing them in 20 mM phosphate buffer, pH 7. The stability of C-PC was assessed by a color change and UV-VIS spectroscopy. Immobilized C-PC was stable under all tested conditions, with only small aggregation and color change appearing
after high-pressure treatment. Immobilization of C-PC by alginate thus shows promise for its efficient stabilization under food processing conditions.
PB  - Wiley
C3  - FEBS Open Bio
T1  - Stabilization of C-phycocyanin by immobilization in alginate beads
VL  - 13
IS  - S2
SP  - 234
EP  - 234
DO  - 10.1002/2211-5463.13646
ER  - 

@conference{
author = "Gligorijević, Nikola and Veličković, Luka and Svrzić, Nikola and Jovanović, Zorana and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "C-Phycocyanin (C-PC), the major protein of cyanobacteria Arthrospira platensis, is a phycobiliprotein with potent biological activity. It has several beneficial effects, including anti-oxidant, anti-inflammatory, immunomodulatory, and anti-cancer. A significant challenge for the broader application of C-PC in the food industry is its stability in food processing conditions, such
as increased light exposure, temperature, and high pressure and drying. This work aimed to investigate if the immobilization of C-PC onto alginate beads could improve its stability. C-PC was
immobilized by dropping the solution of C-PC and 1% alginate (final concentration) in the solution of 2% CaCl2. Both protein/alginate mixture and CaCl2 were kept at pH 4. Immobilized CPC
was treated for 30 min at 65°C, by high pressure up to 4500 bar, and incubated under light exposure for a month. Alginate beads with immobilized C-PC were also left to dry in the fridge and kept for a month. C-PC was extracted from alginate beads by immersing them in 20 mM phosphate buffer, pH 7. The stability of C-PC was assessed by a color change and UV-VIS spectroscopy. Immobilized C-PC was stable under all tested conditions, with only small aggregation and color change appearing
after high-pressure treatment. Immobilization of C-PC by alginate thus shows promise for its efficient stabilization under food processing conditions.",
publisher = "Wiley",
journal = "FEBS Open Bio",
title = "Stabilization of C-phycocyanin by immobilization in alginate beads",
volume = "13",
number = "S2",
pages = "234-234",
doi = "10.1002/2211-5463.13646"
}

Gligorijević, N., Veličković, L., Svrzić, N., Jovanović, Z., Minić, S.,& Nikolić, M.. (2023). Stabilization of C-phycocyanin by immobilization in alginate beads. in FEBS Open Bio
Wiley., 13(S2), 234-234.
https://doi.org/10.1002/2211-5463.13646

Gligorijević N, Veličković L, Svrzić N, Jovanović Z, Minić S, Nikolić M. Stabilization of C-phycocyanin by immobilization in alginate beads. in FEBS Open Bio. 2023;13(S2):234-234.
doi:10.1002/2211-5463.13646 .

Gligorijević, Nikola, Veličković, Luka, Svrzić, Nikola, Jovanović, Zorana, Minić, Simeon, Nikolić, Milan, "Stabilization of C-phycocyanin by immobilization in alginate beads" in FEBS Open Bio, 13, no. S2 (2023):234-234,
https://doi.org/10.1002/2211-5463.13646 . .

TY  - CONF
AU  - Šunderić, Miloš
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Aleksić, Ljubodrag
AU  - Nikolić, Milan
AU  - Takić, Marija
AU  - Minić, Simeon
PY  - 2023
UR  - https://euroanalysis2023.ch/
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6592
AB  - C-Phycocyanin (C-PC) is a phycobiliprotein from cyanobacteria, where it harvests light energy that is then transferred to chlorophylls during photosynthesis. It has an intense blue color due to a covalently bonded tetrapyrrole chromophore, and owing to this property is used in the food industry as a good natural alternative for food coloring. In addition to its coloring properties, C-PC has anti-inflammatory, antioxidant, anti-cancer, and immune-enhancing effects that qualify it as a dietary supplement already included in various formulations, mainly Spirulina extract powders. Since it is used as a food colorant and as a dietary supplement, it may interact with food ingredients, affecting its stability, digestibility, or antioxidant properties. Palmitic acid and linoleic acid (which can be metabolized to linolenic acid) are abundant in meat, milk, and edible oils, so that they could interact with C-PC. C-Phycocyanin isolated from the cyanobacterium Arthrospira platensis (Spirulina) was incubated with increasing concentrations of these three fatty acids, and its fluorescence intensity was monitored. Incubation resulted in a fluorescence quenching effect, indicating that binding had occurred. The binding equations indicated that the association constants were of the same order of magnitude and that the number of approximate binding sites was more than one (Ka = 4.64 x 10⁴ M-¹, n = 1.5 for linoleic acid; Ka = 2.88 x 10⁴ M–¹, n = 1.9 for linolenic acid; Ka = 0.44 x 10⁴ M–¹, n = 0.8 for palmitic acid). This moderate interaction between C-PC and fatty acids could influence its behavior as a nutraceutical and food colorant.
PB  - European Chemical Society
C3  - Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland
T1  - Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study
SP  - 332
EP  - 333
UR  - https://hdl.handle.net/21.15107/rcub_cer_6592
ER  - 

@conference{
author = "Šunderić, Miloš and Veličković, Luka and Gligorijević, Nikola and Aleksić, Ljubodrag and Nikolić, Milan and Takić, Marija and Minić, Simeon",
year = "2023",
abstract = "C-Phycocyanin (C-PC) is a phycobiliprotein from cyanobacteria, where it harvests light energy that is then transferred to chlorophylls during photosynthesis. It has an intense blue color due to a covalently bonded tetrapyrrole chromophore, and owing to this property is used in the food industry as a good natural alternative for food coloring. In addition to its coloring properties, C-PC has anti-inflammatory, antioxidant, anti-cancer, and immune-enhancing effects that qualify it as a dietary supplement already included in various formulations, mainly Spirulina extract powders. Since it is used as a food colorant and as a dietary supplement, it may interact with food ingredients, affecting its stability, digestibility, or antioxidant properties. Palmitic acid and linoleic acid (which can be metabolized to linolenic acid) are abundant in meat, milk, and edible oils, so that they could interact with C-PC. C-Phycocyanin isolated from the cyanobacterium Arthrospira platensis (Spirulina) was incubated with increasing concentrations of these three fatty acids, and its fluorescence intensity was monitored. Incubation resulted in a fluorescence quenching effect, indicating that binding had occurred. The binding equations indicated that the association constants were of the same order of magnitude and that the number of approximate binding sites was more than one (Ka = 4.64 x 10⁴ M-¹, n = 1.5 for linoleic acid; Ka = 2.88 x 10⁴ M–¹, n = 1.9 for linolenic acid; Ka = 0.44 x 10⁴ M–¹, n = 0.8 for palmitic acid). This moderate interaction between C-PC and fatty acids could influence its behavior as a nutraceutical and food colorant.",
publisher = "European Chemical Society",
journal = "Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland",
title = "Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study",
pages = "332-333",
url = "https://hdl.handle.net/21.15107/rcub_cer_6592"
}

Šunderić, M., Veličković, L., Gligorijević, N., Aleksić, L., Nikolić, M., Takić, M.,& Minić, S.. (2023). Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study. in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland
European Chemical Society., 332-333.
https://hdl.handle.net/21.15107/rcub_cer_6592

Šunderić M, Veličković L, Gligorijević N, Aleksić L, Nikolić M, Takić M, Minić S. Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study. in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland. 2023;:332-333.
https://hdl.handle.net/21.15107/rcub_cer_6592 .

Šunderić, Miloš, Veličković, Luka, Gligorijević, Nikola, Aleksić, Ljubodrag, Nikolić, Milan, Takić, Marija, Minić, Simeon, "Dietary fatty acids as a new binding partner of C - phycocyanin: a fluorimetric study" in Euroanalysis 2023 - Analytical Probing of Complex Systems, Abstract book, August 27th - 31st, 2023, Geneva, Switzerland (2023):332-333,
https://hdl.handle.net/21.15107/rcub_cer_6592 .

TY  - CONF
AU  - Ivanov, Aleksandar
AU  - Veličković, Luka
AU  - Jovanović, Zorana
AU  - Gligorijević, Nikola
AU  - Minić, Simeon
AU  - Nikolić, Milan
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6665
AB  - C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Examination of C-phycocyanin interactions with selected vitamins
SP  - 106
EP  - 106
UR  - https://hdl.handle.net/21.15107/rcub_cer_6665
ER  - 

@conference{
author = "Ivanov, Aleksandar and Veličković, Luka and Jovanović, Zorana and Gligorijević, Nikola and Minić, Simeon and Nikolić, Milan",
year = "2023",
abstract = "C-phycocyanin (C-PC) is a photosynthetic protein from Arthrospira platensis
(cyanobacteria). Due to its intense blue colour, which is very rare in nature, C-PC has
industrial applications as a food colourant as a substitute for synthetic food colourants.
Disadvantages of C-PC as a food colourant are its poor stability at high temperatures
(during thermal treatment of the food) and its sensibility to change pH value. The binding
of food-derived small molecules, such as vitamins, could stabilize the structure of C-PC at
high temperatures and wide pH ranges. In this study, we characterized the binding of
selected vitamins to C-PC, purified from the commercial powder of Arthrospira platensis.
We used hydrophilic vitamins (B1, B2, B7, B9, B12), lipophilic vitamins (A, D3) and
provitamin (β-carotene). Fluorescent spectroscopy showed a decrease in fluorescence of CPC
i n t he p resence o f v itamin A, v itamin D3 a nd β -carotene (lipophilic molecules)
compared to the control. In contrast, the fluorescence of C-PC in the presence of
hydrophilic vitamins showed minimal change. The protein fluorescence quenching
approach demonstrated hydrophobic (pro)vitamins binding affinities ranging from 0.02 to
5.9 x 105 M-1, with the ability of hydrophobic (pro)vitamins to bind at the different sites on
C-PC. UV-VIS spectrophotometry showed that the binding of hydrophobic (pro)vitamins
does not affect the protein colour, while CD spectroscopy revealed that the binding of
chosen molecules does not significantly influence the secondary structure of C-PC.
Overall, this study demonstrated C-PC's significant potential in binding hydrophobic
(pro)vitamins, while further research is required to test if these ligands could improve CPC
stability.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Examination of C-phycocyanin interactions with selected vitamins",
pages = "106-106",
url = "https://hdl.handle.net/21.15107/rcub_cer_6665"
}

Ivanov, A., Veličković, L., Jovanović, Z., Gligorijević, N., Minić, S.,& Nikolić, M.. (2023). Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665

Ivanov A, Veličković L, Jovanović Z, Gligorijević N, Minić S, Nikolić M. Examination of C-phycocyanin interactions with selected vitamins. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:106-106.
https://hdl.handle.net/21.15107/rcub_cer_6665 .

Ivanov, Aleksandar, Veličković, Luka, Jovanović, Zorana, Gligorijević, Nikola, Minić, Simeon, Nikolić, Milan, "Examination of C-phycocyanin interactions with selected vitamins" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):106-106,
https://hdl.handle.net/21.15107/rcub_cer_6665 .

TY  - CONF
AU  - Aleksić, Ljubodrag
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Šunderić, Miloš
AU  - Takić, Marija
AU  - Nikolić, Milan
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6667
AB  - Cultured meat requires less land and water and is less polluting, but still costly. The critical
challenge in cultivated meat science is identifying and developing bovine serum albumin
alternatives as the key component in cell media. Phycobiliproteins (PBPs) from micro- and
macroalgae are promising candidates for albumin replacement due to their high abundance
and well-known excellent antioxidative and metal-binding activities of covalently attached
tetrapyrrole chromophores. Considering the importance of fatty acids (FA) binding by
albumin for cell cultivation, the additional prerequisites for developing PBPs as albumin
replacement components is their validation for the ability to bind FA. This study aims to
examine the ability of C-phycocyanin (C-PC), the major PBP of microalgae Arthrospira
platensis, to bind seven fatty acids (stearic, palmitic, oleic, elaidic, linoleic, linolenic and
docosahexaenoic acid). For this purpose, we employed various optical spectroscopy
techniques (fluorescence, CD, and VIS absorption spectroscopy). The protein fluorescence
quenching approach demonstrated FA binding affinities ranging from 0.42 to 2.4 x 105
M−1, with the ability of FA to bind at different sites on C-PC. Fatty acid binding induces
substantial changes in the VIS absorption spectra of C-PC, indicating the FA are attached
in the vicinity of C-PC chromophores. On the other hand, CD spectroscopy did not show
significant effects of FA binding on C-PC secondary structure content. Overall, this study
revealed C-PC's significant potential in binding FA, the critical prerequisite to replacing
albumin for developing animal-free cell media for meat cultivation.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin
SP  - 121
EP  - 121
UR  - https://hdl.handle.net/21.15107/rcub_cer_6667
ER  - 

@conference{
author = "Aleksić, Ljubodrag and Veličković, Luka and Gligorijević, Nikola and Šunderić, Miloš and Takić, Marija and Nikolić, Milan and Minić, Simeon",
year = "2023",
abstract = "Cultured meat requires less land and water and is less polluting, but still costly. The critical
challenge in cultivated meat science is identifying and developing bovine serum albumin
alternatives as the key component in cell media. Phycobiliproteins (PBPs) from micro- and
macroalgae are promising candidates for albumin replacement due to their high abundance
and well-known excellent antioxidative and metal-binding activities of covalently attached
tetrapyrrole chromophores. Considering the importance of fatty acids (FA) binding by
albumin for cell cultivation, the additional prerequisites for developing PBPs as albumin
replacement components is their validation for the ability to bind FA. This study aims to
examine the ability of C-phycocyanin (C-PC), the major PBP of microalgae Arthrospira
platensis, to bind seven fatty acids (stearic, palmitic, oleic, elaidic, linoleic, linolenic and
docosahexaenoic acid). For this purpose, we employed various optical spectroscopy
techniques (fluorescence, CD, and VIS absorption spectroscopy). The protein fluorescence
quenching approach demonstrated FA binding affinities ranging from 0.42 to 2.4 x 105
M−1, with the ability of FA to bind at different sites on C-PC. Fatty acid binding induces
substantial changes in the VIS absorption spectra of C-PC, indicating the FA are attached
in the vicinity of C-PC chromophores. On the other hand, CD spectroscopy did not show
significant effects of FA binding on C-PC secondary structure content. Overall, this study
revealed C-PC's significant potential in binding FA, the critical prerequisite to replacing
albumin for developing animal-free cell media for meat cultivation.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin",
pages = "121-121",
url = "https://hdl.handle.net/21.15107/rcub_cer_6667"
}

Aleksić, L., Veličković, L., Gligorijević, N., Šunderić, M., Takić, M., Nikolić, M.,& Minić, S.. (2023). Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 121-121.
https://hdl.handle.net/21.15107/rcub_cer_6667

Aleksić L, Veličković L, Gligorijević N, Šunderić M, Takić M, Nikolić M, Minić S. Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:121-121.
https://hdl.handle.net/21.15107/rcub_cer_6667 .

Aleksić, Ljubodrag, Veličković, Luka, Gligorijević, Nikola, Šunderić, Miloš, Takić, Marija, Nikolić, Milan, Minić, Simeon, "Examining fatty acid interactions with Arthrospira platensis-derived C-phycocyanin" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):121-121,
https://hdl.handle.net/21.15107/rcub_cer_6667 .

TY  - CONF
AU  - Jovanović, Zorana
AU  - Annighöfer, Burkhard
AU  - Dudzinski, Daniel
AU  - Veličković, Luka
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Brûlet, Annie
AU  - Assifaoui, Ali
AU  - Combet, Sophie
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6669
AB  - The color of food products is an important aspect in food industry, and its preservation
remains a big challenge. We aim to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae. For this purpose, we incorporated C-PC in
combined starch and β-lactoglobulin (BLG) hydrogels by using a high-pressure (HP)
process. Indeed, in thermal treatment, the color derived from C-PC is entirely lost. We
characterized the obtained HP gels by both rheology and small-angle X-ray scattering
(SAXS). Various formulations of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were tested under HP up to 4,500 bar. A good preservation of the C-PC pigment
was established by mixing BLG and starch with C-PC at pH 7, with concentrations of 180,
5, and 10 mg/mL, respectively. Identical component concentrations were maintained in the
binary systems. Structure of gels was characterized by SAXS providing insight of C-PC
interactions with BLG and starch after HP process which leads to the formation of solid
gels with larger mesh compared to two-component systems. This results in enhanced
mechanical properties, which were determined by amplitude and frequency sweep
measurements using a rheometer with applied plane/plane geometry. Therefore, adding
starch, even at small concentration, significantly improves gel visual appearance and
mechanical properties. Our study reveals that preservation through HP treatment is more
effective than high temperature treatment, as visually observed through the sustained color
integrity of C-PC blue dye.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin
SP  - 150
EP  - 150
UR  - https://hdl.handle.net/21.15107/rcub_cer_6669
ER  - 

@conference{
author = "Jovanović, Zorana and Annighöfer, Burkhard and Dudzinski, Daniel and Veličković, Luka and Gligorijević, Nikola and Nikolić, Milan and Brûlet, Annie and Assifaoui, Ali and Combet, Sophie and Minić, Simeon",
year = "2023",
abstract = "The color of food products is an important aspect in food industry, and its preservation
remains a big challenge. We aim to preserve the natural blue dye of C-phycocyanin (C-PC)
phycobiliprotein from Spirulina microalgae. For this purpose, we incorporated C-PC in
combined starch and β-lactoglobulin (BLG) hydrogels by using a high-pressure (HP)
process. Indeed, in thermal treatment, the color derived from C-PC is entirely lost. We
characterized the obtained HP gels by both rheology and small-angle X-ray scattering
(SAXS). Various formulations of binary (BLG/C-PC) and ternary (starch/BLG/C-PC)
systems were tested under HP up to 4,500 bar. A good preservation of the C-PC pigment
was established by mixing BLG and starch with C-PC at pH 7, with concentrations of 180,
5, and 10 mg/mL, respectively. Identical component concentrations were maintained in the
binary systems. Structure of gels was characterized by SAXS providing insight of C-PC
interactions with BLG and starch after HP process which leads to the formation of solid
gels with larger mesh compared to two-component systems. This results in enhanced
mechanical properties, which were determined by amplitude and frequency sweep
measurements using a rheometer with applied plane/plane geometry. Therefore, adding
starch, even at small concentration, significantly improves gel visual appearance and
mechanical properties. Our study reveals that preservation through HP treatment is more
effective than high temperature treatment, as visually observed through the sustained color
integrity of C-PC blue dye.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin",
pages = "150-150",
url = "https://hdl.handle.net/21.15107/rcub_cer_6669"
}

Jovanović, Z., Annighöfer, B., Dudzinski, D., Veličković, L., Gligorijević, N., Nikolić, M., Brûlet, A., Assifaoui, A., Combet, S.,& Minić, S.. (2023). Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 150-150.
https://hdl.handle.net/21.15107/rcub_cer_6669

Jovanović Z, Annighöfer B, Dudzinski D, Veličković L, Gligorijević N, Nikolić M, Brûlet A, Assifaoui A, Combet S, Minić S. Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:150-150.
https://hdl.handle.net/21.15107/rcub_cer_6669 .

Jovanović, Zorana, Annighöfer, Burkhard, Dudzinski, Daniel, Veličković, Luka, Gligorijević, Nikola, Nikolić, Milan, Brûlet, Annie, Assifaoui, Ali, Combet, Sophie, Minić, Simeon, "Combined hydrogels of starch and β-lactoglobulin as matrices for the preservation of C-phycocyanin" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):150-150,
https://hdl.handle.net/21.15107/rcub_cer_6669 .

TY  - CONF
AU  - Veličković, Luka
AU  - Sibinčić, Nikolina
AU  - Stojadinović, Marija
AU  - Gligorijević, Nikola
AU  - Nikolić, Milan
AU  - Srdić, Tatjana
AU  - Minić, Simeon
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6671
AB  - This study investigates the impact of Porphyra sp. extracts on HT29 cell line growth and
viability at reduced serum conditions. The concentration-dependent effects of
phycobiliproteins (PBPs) on cell proliferation were examined over various time intervals.
Lower concentrations of PBPs (20 μg/mL) demonstrated an increase in HT29 cell viability
after 48 hours and 5 days of cultivation at reduced serum concentration (final serum
concentration was in the range from 5 to 8%). This suggests a potential positive influence
on cell proliferation, likely due to their antioxidant properties. Conversely, higher
concentrations of PBPs exhibited inhibitory effects on cell growth, possibly due to
cytotoxicity at elevated levels. Remarkably, when HT29 cells were cultured solely in algal
extract without fetal calf serum (FCS), complete growth inhibition was observed after 72
hours. This finding underscores the insufficient nutrient and growth factor provision of
PBPs alone for sustaining cell viability. Morphological differences observed in cells
cultured with 70 μg/mL of PBPs indicated potential alterations in cellular morphology.
Notably, 70 μg/mL of PBPs in RPMI medium with 5% FCS displayed growth inhibition
compared to the control (5% FCS). Furthermore, we assessed HT29 cell adaptability to
changes in FCS concentration and PBP supplementation. Cells incubated under varying
FCS and PBP conditions were subcultured into RPMI medium with lower FCS
concentration and PBPs from Porphyra. The viability of cells following subculturing
indicated sustained adaptability to reduced FCS levels. Overall, this study provides
valuable insights into the concentration-dependent effects of PBPs from Porphyra extracts
on HT29 cell growth and viability. The findings underscore the potential benefits of PBPs
at lower concentrations for cell proliferation at reduced serum conditions and reveal the
adaptability of HT29 cells to changing culture conditions.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture
SP  - 82
EP  - 82
UR  - https://hdl.handle.net/21.15107/rcub_cer_6671
ER  - 

@conference{
author = "Veličković, Luka and Sibinčić, Nikolina and Stojadinović, Marija and Gligorijević, Nikola and Nikolić, Milan and Srdić, Tatjana and Minić, Simeon",
year = "2023",
abstract = "This study investigates the impact of Porphyra sp. extracts on HT29 cell line growth and
viability at reduced serum conditions. The concentration-dependent effects of
phycobiliproteins (PBPs) on cell proliferation were examined over various time intervals.
Lower concentrations of PBPs (20 μg/mL) demonstrated an increase in HT29 cell viability
after 48 hours and 5 days of cultivation at reduced serum concentration (final serum
concentration was in the range from 5 to 8%). This suggests a potential positive influence
on cell proliferation, likely due to their antioxidant properties. Conversely, higher
concentrations of PBPs exhibited inhibitory effects on cell growth, possibly due to
cytotoxicity at elevated levels. Remarkably, when HT29 cells were cultured solely in algal
extract without fetal calf serum (FCS), complete growth inhibition was observed after 72
hours. This finding underscores the insufficient nutrient and growth factor provision of
PBPs alone for sustaining cell viability. Morphological differences observed in cells
cultured with 70 μg/mL of PBPs indicated potential alterations in cellular morphology.
Notably, 70 μg/mL of PBPs in RPMI medium with 5% FCS displayed growth inhibition
compared to the control (5% FCS). Furthermore, we assessed HT29 cell adaptability to
changes in FCS concentration and PBP supplementation. Cells incubated under varying
FCS and PBP conditions were subcultured into RPMI medium with lower FCS
concentration and PBPs from Porphyra. The viability of cells following subculturing
indicated sustained adaptability to reduced FCS levels. Overall, this study provides
valuable insights into the concentration-dependent effects of PBPs from Porphyra extracts
on HT29 cell growth and viability. The findings underscore the potential benefits of PBPs
at lower concentrations for cell proliferation at reduced serum conditions and reveal the
adaptability of HT29 cells to changing culture conditions.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture",
pages = "82-82",
url = "https://hdl.handle.net/21.15107/rcub_cer_6671"
}

Veličković, L., Sibinčić, N., Stojadinović, M., Gligorijević, N., Nikolić, M., Srdić, T.,& Minić, S.. (2023). Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 82-82.
https://hdl.handle.net/21.15107/rcub_cer_6671

Veličković L, Sibinčić N, Stojadinović M, Gligorijević N, Nikolić M, Srdić T, Minić S. Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:82-82.
https://hdl.handle.net/21.15107/rcub_cer_6671 .

Veličković, Luka, Sibinčić, Nikolina, Stojadinović, Marija, Gligorijević, Nikola, Nikolić, Milan, Srdić, Tatjana, Minić, Simeon, "Exploring if Porphyra sp. extract functions as serum substitute in HT29 cell culture" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):82-82,
https://hdl.handle.net/21.15107/rcub_cer_6671 .

TY  - CONF
AU  - Radović, Jelena
AU  - Popović, Dragana
AU  - Ćurčić, Tatjana
AU  - Nikolić, Milan
AU  - Minić, Simeon
AU  - Gligorijević, Nikola
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6666
AB  - This study aimed to improve chitosan polymer's capabilities to absorb mercury by
immobilising phycobiliproteins (PBPs) onto the surface of chitosan beads (chitosan–
PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have
several industrially essential applications. These proteins can bind heavy metals with high
affinities. Protein extracts obtained from both Arthrospira platensis, with C-phycocyanin
as the dominant phycobiliprotein and Neoporphyra haitanensis, with R-phycocyanin and
R-phycoerythrin as the dominant PBPs, were covalently immobilised onto chitosan beads.
Binding analysis showed that, on average, 54 μg of PBPs were immobilised per bead.
Immobilised proteins were still in their native state, with no visible colour change after
immobilisation. Chitosan–PBPs and chitosan alone were tested for mercury adsorption at
pH 4 and pH 7 by atomic absorption spectroscopy. The tested concentration range of
mercury was from 1 to 70 ppm. Affinity, calculated using Henry's binding isotherm, of
chitosan–PBPs for mercury was higher at both pH values than chitosan alone.
Furthermore, chitosan–PBPs beads were able to absorb significantly more mercury than
chitosan alone. These results show that the covalent immobilisation of PBPs onto chitosan
improves its mercury adsorption characteristics and creates a more efficient eco-friendly
adsorbent for removing mercury ions in the tested concentration range.
PB  - Serbian Biochemical Society
C3  - Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
T1  - Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal
SP  - 116
EP  - 116
UR  - https://hdl.handle.net/21.15107/rcub_cer_6666
ER  - 

@conference{
author = "Radović, Jelena and Popović, Dragana and Ćurčić, Tatjana and Nikolić, Milan and Minić, Simeon and Gligorijević, Nikola",
year = "2023",
abstract = "This study aimed to improve chitosan polymer's capabilities to absorb mercury by
immobilising phycobiliproteins (PBPs) onto the surface of chitosan beads (chitosan–
PBPs). Phycobiliproteins, light-harvesting proteins from algae and cyanobacteria, have
several industrially essential applications. These proteins can bind heavy metals with high
affinities. Protein extracts obtained from both Arthrospira platensis, with C-phycocyanin
as the dominant phycobiliprotein and Neoporphyra haitanensis, with R-phycocyanin and
R-phycoerythrin as the dominant PBPs, were covalently immobilised onto chitosan beads.
Binding analysis showed that, on average, 54 μg of PBPs were immobilised per bead.
Immobilised proteins were still in their native state, with no visible colour change after
immobilisation. Chitosan–PBPs and chitosan alone were tested for mercury adsorption at
pH 4 and pH 7 by atomic absorption spectroscopy. The tested concentration range of
mercury was from 1 to 70 ppm. Affinity, calculated using Henry's binding isotherm, of
chitosan–PBPs for mercury was higher at both pH values than chitosan alone.
Furthermore, chitosan–PBPs beads were able to absorb significantly more mercury than
chitosan alone. These results show that the covalent immobilisation of PBPs onto chitosan
improves its mercury adsorption characteristics and creates a more efficient eco-friendly
adsorbent for removing mercury ions in the tested concentration range.",
publisher = "Serbian Biochemical Society",
journal = "Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia",
title = "Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal",
pages = "116-116",
url = "https://hdl.handle.net/21.15107/rcub_cer_6666"
}

Radović, J., Popović, D., Ćurčić, T., Nikolić, M., Minić, S.,& Gligorijević, N.. (2023). Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia
Serbian Biochemical Society., 116-116.
https://hdl.handle.net/21.15107/rcub_cer_6666

Radović J, Popović D, Ćurčić T, Nikolić M, Minić S, Gligorijević N. Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal. in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia. 2023;:116-116.
https://hdl.handle.net/21.15107/rcub_cer_6666 .

Radović, Jelena, Popović, Dragana, Ćurčić, Tatjana, Nikolić, Milan, Minić, Simeon, Gligorijević, Nikola, "Applying immobilised phycobiliproteins onto chitosan for efficient mercury removal" in Serbian Biochemical Society Twelfth Conference, International scientific meeting, “Biochemistry in Biotechnology,” September 21-23, 2023, Belgrade, Serbia (2023):116-116,
https://hdl.handle.net/21.15107/rcub_cer_6666 .

TY  - CONF
AU  - Perić, Marko
AU  - Vuković, George
AU  - Knežević, Sanja
AU  - Nikolić, Milan
AU  - Šuljagić, Marija
AU  - Anđelković, Ljubica
AU  - Nenadović, Snežana
AU  - Ivanović, Marija
AU  - Mirković, Miljana
AU  - Pavlović, Vladmir B.
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6022
AB  - Radiation shielding is a crucial precautionary measure in decreasing the dose of exposure medical personnel experience. The physical dimensions of these shields, specifically thickness and shape, are dependent on the type of radiation, energy and specific radioactivity. Currently, the most common radiation shielding equipment is made of lead, tungsten or uranium. Although these heavy metals have favorable shielding properties against ionizing radiation, protective garments such as lead aprons are heavy to wear and can pose significant health risks. Taking this into account, the primary goal of this study is to understand the radiation shielding properties of lead-free polymer geopolymer-polyurethane based composites. The geopolymer was synthesized using an 80%-20% mixture of fly ash and a bio-polyol substrate which was subsequently homogenized using MDI44. As a result, 6 samples of the geopolymer-polyurethane based composites were fabricated of which 5 were 90%-10% compositions between the mixture and varying concentrations of BaSO4 and Bi2O3 respectively. The last sample consisted of the pure fly ash/bio-polyol mixture. XRF and ICP analysis was used to chemically characterize the fly ash. The composite structures were analyzed using XRD, while the microstructural morphology was investigated using SEM techniques. Utilizing an energy-dispersive x-ray spectrometer (EDS), elemental abundance and agglomerating behavior was analyzed for each composite variant. The X-ray attenuation measurements pointed out that the obtained composites have the potential for a design of lead-free protective clothing against X-ray shielding in medical applications.
PB  - Bucharest: SRMNIM
C3  - Abstracts E-Book, 10th Balkan Congress of Nuclear Medicine & 5th Romanian Congress of Nuclear Medicine, 15-18 March, 2023, Bucharest, Romania
T1  - Lead Free Polymer Composites for Radiation Shielding
SP  - 17
SP  - 17
UR  - https://hdl.handle.net/21.15107/rcub_cer_6022
ER  - 

@conference{
author = "Perić, Marko and Vuković, George and Knežević, Sanja and Nikolić, Milan and Šuljagić, Marija and Anđelković, Ljubica and Nenadović, Snežana and Ivanović, Marija and Mirković, Miljana and Pavlović, Vladmir B.",
year = "2023",
abstract = "Radiation shielding is a crucial precautionary measure in decreasing the dose of exposure medical personnel experience. The physical dimensions of these shields, specifically thickness and shape, are dependent on the type of radiation, energy and specific radioactivity. Currently, the most common radiation shielding equipment is made of lead, tungsten or uranium. Although these heavy metals have favorable shielding properties against ionizing radiation, protective garments such as lead aprons are heavy to wear and can pose significant health risks. Taking this into account, the primary goal of this study is to understand the radiation shielding properties of lead-free polymer geopolymer-polyurethane based composites. The geopolymer was synthesized using an 80%-20% mixture of fly ash and a bio-polyol substrate which was subsequently homogenized using MDI44. As a result, 6 samples of the geopolymer-polyurethane based composites were fabricated of which 5 were 90%-10% compositions between the mixture and varying concentrations of BaSO4 and Bi2O3 respectively. The last sample consisted of the pure fly ash/bio-polyol mixture. XRF and ICP analysis was used to chemically characterize the fly ash. The composite structures were analyzed using XRD, while the microstructural morphology was investigated using SEM techniques. Utilizing an energy-dispersive x-ray spectrometer (EDS), elemental abundance and agglomerating behavior was analyzed for each composite variant. The X-ray attenuation measurements pointed out that the obtained composites have the potential for a design of lead-free protective clothing against X-ray shielding in medical applications.",
publisher = "Bucharest: SRMNIM",
journal = "Abstracts E-Book, 10th Balkan Congress of Nuclear Medicine & 5th Romanian Congress of Nuclear Medicine, 15-18 March, 2023, Bucharest, Romania",
title = "Lead Free Polymer Composites for Radiation Shielding",
pages = "17-17",
url = "https://hdl.handle.net/21.15107/rcub_cer_6022"
}

Perić, M., Vuković, G., Knežević, S., Nikolić, M., Šuljagić, M., Anđelković, L., Nenadović, S., Ivanović, M., Mirković, M.,& Pavlović, V. B.. (2023). Lead Free Polymer Composites for Radiation Shielding. in Abstracts E-Book, 10th Balkan Congress of Nuclear Medicine & 5th Romanian Congress of Nuclear Medicine, 15-18 March, 2023, Bucharest, Romania
Bucharest: SRMNIM., 17.
https://hdl.handle.net/21.15107/rcub_cer_6022

Perić M, Vuković G, Knežević S, Nikolić M, Šuljagić M, Anđelković L, Nenadović S, Ivanović M, Mirković M, Pavlović VB. Lead Free Polymer Composites for Radiation Shielding. in Abstracts E-Book, 10th Balkan Congress of Nuclear Medicine & 5th Romanian Congress of Nuclear Medicine, 15-18 March, 2023, Bucharest, Romania. 2023;:17.
https://hdl.handle.net/21.15107/rcub_cer_6022 .

Perić, Marko, Vuković, George, Knežević, Sanja, Nikolić, Milan, Šuljagić, Marija, Anđelković, Ljubica, Nenadović, Snežana, Ivanović, Marija, Mirković, Miljana, Pavlović, Vladmir B., "Lead Free Polymer Composites for Radiation Shielding" in Abstracts E-Book, 10th Balkan Congress of Nuclear Medicine & 5th Romanian Congress of Nuclear Medicine, 15-18 March, 2023, Bucharest, Romania (2023):17,
https://hdl.handle.net/21.15107/rcub_cer_6022 .

TY  - JOUR
AU  - Nikolić Kokić, Aleksandra
AU  - Tatalović, Nikola
AU  - Brkljačić, Jelena
AU  - Mijović, Milica
AU  - Nestorović, Vojkan
AU  - Mijušković, Ana
AU  - Oreščanin-Dušić, Zorana
AU  - Vidonja Uzelac, Teodora
AU  - Nikolić, Milan
AU  - Spasić, Snežana
AU  - Blagojević, Duško
AU  - Miljević, Čedo
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5557
AB  - Sexual dysfunction, as a noticeable adverse effect of atypical antipsychotic drugs (APDs)
for the treatment of schizophrenia, has not been investigated in detail. A study was undertaken
to investigate whether 28-day long treatment with clozapine, ziprasidone or sertindole (using a
recommended daily dose for atypical antipsychotic therapy), induced histopathological changes
both in rat testicles and prostate, changed the activity of the antioxidant defence system and altered blood testosterone and prolactin. Clozapine, ziprasidone and sertindole induced histopathological changes in rat testicular tissue, which could be attributed to a disturbed testicular antioxidant defence system in addition to an altered prolactin to testosterone ratio. None of the APD treatments induced histopathological changes in prostate. Our results demonstrate that APDs have the capacity to change both redox and endocrinological balance. One or both outcomes could underline testicular degeneration and disturbed spermatogenesis.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Antipsychotic Drug-Mediated Adverse Effects on Rat Testicles May Be Caused by Altered Redox and Hormonal Homeostasis
VL  - 23
IS  - 22
SP  - 13698
DO  - 10.3390/ijms232213698
ER  - 

@article{
author = "Nikolić Kokić, Aleksandra and Tatalović, Nikola and Brkljačić, Jelena and Mijović, Milica and Nestorović, Vojkan and Mijušković, Ana and Oreščanin-Dušić, Zorana and Vidonja Uzelac, Teodora and Nikolić, Milan and Spasić, Snežana and Blagojević, Duško and Miljević, Čedo",
year = "2022",
abstract = "Sexual dysfunction, as a noticeable adverse effect of atypical antipsychotic drugs (APDs)
for the treatment of schizophrenia, has not been investigated in detail. A study was undertaken
to investigate whether 28-day long treatment with clozapine, ziprasidone or sertindole (using a
recommended daily dose for atypical antipsychotic therapy), induced histopathological changes
both in rat testicles and prostate, changed the activity of the antioxidant defence system and altered blood testosterone and prolactin. Clozapine, ziprasidone and sertindole induced histopathological changes in rat testicular tissue, which could be attributed to a disturbed testicular antioxidant defence system in addition to an altered prolactin to testosterone ratio. None of the APD treatments induced histopathological changes in prostate. Our results demonstrate that APDs have the capacity to change both redox and endocrinological balance. One or both outcomes could underline testicular degeneration and disturbed spermatogenesis.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Antipsychotic Drug-Mediated Adverse Effects on Rat Testicles May Be Caused by Altered Redox and Hormonal Homeostasis",
volume = "23",
number = "22",
pages = "13698",
doi = "10.3390/ijms232213698"
}

Nikolić Kokić, A., Tatalović, N., Brkljačić, J., Mijović, M., Nestorović, V., Mijušković, A., Oreščanin-Dušić, Z., Vidonja Uzelac, T., Nikolić, M., Spasić, S., Blagojević, D.,& Miljević, Č.. (2022). Antipsychotic Drug-Mediated Adverse Effects on Rat Testicles May Be Caused by Altered Redox and Hormonal Homeostasis. in International Journal of Molecular Sciences
MDPI., 23(22), 13698.
https://doi.org/10.3390/ijms232213698

Nikolić Kokić A, Tatalović N, Brkljačić J, Mijović M, Nestorović V, Mijušković A, Oreščanin-Dušić Z, Vidonja Uzelac T, Nikolić M, Spasić S, Blagojević D, Miljević Č. Antipsychotic Drug-Mediated Adverse Effects on Rat Testicles May Be Caused by Altered Redox and Hormonal Homeostasis. in International Journal of Molecular Sciences. 2022;23(22):13698.
doi:10.3390/ijms232213698 .

Nikolić Kokić, Aleksandra, Tatalović, Nikola, Brkljačić, Jelena, Mijović, Milica, Nestorović, Vojkan, Mijušković, Ana, Oreščanin-Dušić, Zorana, Vidonja Uzelac, Teodora, Nikolić, Milan, Spasić, Snežana, Blagojević, Duško, Miljević, Čedo, "Antipsychotic Drug-Mediated Adverse Effects on Rat Testicles May Be Caused by Altered Redox and Hormonal Homeostasis" in International Journal of Molecular Sciences, 23, no. 22 (2022):13698,
https://doi.org/10.3390/ijms232213698 . .